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{{PBB|geneid=397}}
{{PBB|geneid=397}}
'''Rho GDP-dissociation inhibitor 2''' is a [[protein]] that in humans is encoded by the ''ARHGDIB'' [[gene]].<ref name="pmid8434008">{{cite journal | author = Lelias JM, Adra CN, Wulf GM, Guillemot JC, Khagad M, Caput D, Lim B | title = cDNA cloning of a human mRNA preferentially expressed in hematopoietic cells and with homology to a GDP-dissociation inhibitor for the rho GTP-binding proteins | journal = Proc Natl Acad Sci U S A | volume = 90 | issue = 4 | pages = 1479–83 | year = 1993 | month = March | pmid = 8434008 | pmc = 45897 | doi =10.1073/pnas.90.4.1479 }}</ref><ref name="pmid8356058">{{cite journal | author = Scherle P, Behrens T, Staudt LM | title = Ly-GDI, a GDP-dissociation inhibitor of the RhoA GTP-binding protein, is expressed preferentially in lymphocytes | journal = Proc Natl Acad Sci U S A | volume = 90 | issue = 16 | pages = 7568–72 | year = 1993 | month = September | pmid = 8356058 | pmc = 47183 | doi =10.1073/pnas.90.16.7568 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ARHGDIB Rho GDP dissociation inhibitor (GDI) beta| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=397| accessdate = }}</ref>. Aliases of this gene include ''RhoGDI2'', ''GDID4'', ''Rho GDI 2'', and others <ref>{{cite web|url=http://www.genecards.org/index.php?path=/Search/keyword/ARHGDIB}}</ref>.
'''Rho GDP-dissociation inhibitor 2''' is a [[protein]] that in humans is encoded by the ''ARHGDIB'' [[gene]].<ref name="pmid8434008">{{cite journal | author = Lelias JM, Adra CN, Wulf GM, Guillemot JC, Khagad M, Caput D, Lim B | title = cDNA cloning of a human mRNA preferentially expressed in hematopoietic cells and with homology to a GDP-dissociation inhibitor for the rho GTP-binding proteins | journal = Proc Natl Acad Sci U S A | volume = 90 | issue = 4 | pages = 1479–83 | year = 1993 | month = March | pmid = 8434008 | pmc = 45897 | doi =10.1073/pnas.90.4.1479 }}</ref><ref name="pmid8356058">{{cite journal | author = Scherle P, Behrens T, Staudt LM | title = Ly-GDI, a GDP-dissociation inhibitor of the RhoA GTP-binding protein, is expressed preferentially in lymphocytes | journal = Proc Natl Acad Sci U S A | volume = 90 | issue = 16 | pages = 7568–72 | year = 1993 | month = September | pmid = 8356058 | pmc = 47183 | doi =10.1073/pnas.90.16.7568 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ARHGDIB Rho GDP dissociation inhibitor (GDI) beta| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=397| accessdate = }}</ref>. Aliases of this gene include ''RhoGDI2'', ''GDID4'', ''Rho GDI 2'', and others <ref>{{cite web|title = "Gene Cards: ARHGDIB | url=http://www.genecards.org/index.php?path=/Search/keyword/ARHGDIB}}</ref>.


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==Gene Family ==
==Gene Family ==
RhoGDI2 (ARHGDIB) is part of a family of three members: RhoGDI1, RhoGDI2 (also known as RhoGDIB, D4-GDI or Ly-GDI) and RhoGDI3. RhoGDI1 is expressed in many organs and is the best studied member of the family.<ref>{{cite journal|last=DerMardirossian|first=Céline|coauthors=Bokoch, Gary M.|title=GDIs: central regulatory molecules in Rho GTPase activation|journal=Trends in Cell Biology|date=NaN undefined NaN|volume=15|issue=7|pages=356–363|doi=doi:10.1016/j.tcb.2005.05.001}}</ref> <ref>{{cite journal|last=Dovas|first=Athanassios|coauthors=Couchman, John R.|title=RhoGDI: multiple functions in the regulation of Rho family GTPase activities|journal=Biochemical Journal|date=NaN undefined NaN|volume=390|issue=1|pages=1|doi=10.1042/BJ20050104}}</ref> <ref>{{cite journal|last=Garcia-Mata|first=Rafael|coauthors=Boulter, Etienne; Burridge, Keith|title=The 'invisible hand': regulation of RHO GTPases by RHOGDIs|journal=Nature Reviews Molecular Cell Biology|date=NaN undefined NaN|volume=12|issue=8|pages=493–504|doi=10.1038/nrm3153}}</ref> RhoGDI2 was initially believed to be expressed specifically in blood forming cells <ref>{{cite journal|last=Scherle|first=P|coauthors=Behrens, T; Staudt, LM|title=Ly-GDI, a GDP-dissociation inhibitor of the RhoA GTP-binding protein, is expressed preferentially in lymphocytes.|journal=Proceedings of the National Academy of Sciences of the United States of America|date=1993 Aug 15|volume=90|issue=16|pages=7568-72|pmid=8356058}}</ref> , but has subsequently been found to be highly expressed in a variety of other cell types as well <ref>{{cite journal|last=Theodorescu|first=D.|title=Reduced Expression of Metastasis Suppressor RhoGDI2 Is Associated with Decreased Survival for Patients with Bladder Cancer|journal=Clinical Cancer Research|date=1 June 2004|volume=10|issue=11|pages=3800–3806|doi=10.1158/1078-0432.CCR-03-0653}}</ref> . RhoGDI3 is predominantly expressed in brain, lung, kidney, testis and pancreas <ref>{{cite journal|last=Adra|first=CN|coauthors=Manor, D; Ko, JL; Zhu, S; Horiuchi, T; Van Aelst, L; Cerione, RA; Lim, B|title=RhoGDIgamma: a GDP-dissociation inhibitor for Rho proteins with preferential expression in brain and pancreas.|journal=Proceedings of the National Academy of Sciences of the United States of America|date=1997 Apr 29|volume=94|issue=9|pages=4279-84|pmid=9113980}}</ref> <ref>{{cite journal|last=Zalcman|first=G|coauthors=Closson, V; Camonis, J; Honoré, N; Rousseau-Merck, MF; Tavitian, A; Olofsson, B|title=RhoGDI-3 is a new GDP dissociation inhibitor (GDI). Identification of a non-cytosolic GDI protein interacting with the small GTP-binding proteins RhoB and RhoG.|journal=The Journal of biological chemistry|date=1996 Nov 29|volume=271|issue=48|pages=30366-74|pmid=8939998}}</ref> , and is targeted to specific parts of the cell such as the Golgi where it may play a role in transport or proteins in cells. <ref>{{cite journal|last=Brunet|first=N|coauthors=Morin, A; Olofsson, B|title=RhoGDI-3 regulates RhoG and targets this protein to the Golgi complex through its unique N-terminal domain.|journal=Traffic (Copenhagen, Denmark)|date=2002 May|volume=3|issue=5|pages=342-57|pmid=11967128}}</ref> <ref>{{cite journal|last=Dransart|first=E|coauthors=Morin, A; Cherfils, J; Olofsson, B|title=Uncoupling of inhibitory and shuttling functions of rho GDP dissociation inhibitors.|journal=The Journal of biological chemistry|date=2005 Feb 11|volume=280|issue=6|pages=4674-83|pmid=15513926}}</ref>.
RhoGDI2 (ARHGDIB) is part of a family of three members: RhoGDI1, RhoGDI2 (also known as RhoGDIB, D4-GDI or Ly-GDI) and RhoGDI3. RhoGDI1 is expressed in many organs and is the best studied member of the family.<ref>{{cite journal|last=DerMardirossian|first=Céline|coauthors=Bokoch, Gary M.|title=GDIs: central regulatory molecules in Rho GTPase activation|journal=Trends in Cell Biology|date=NaN undefined NaN|volume=15|issue=7|pages=356–363|doi=doi:10.1016/j.tcb.2005.05.001}}</ref> <ref>{{cite journal|last=Dovas|first=Athanassios|coauthors=Couchman, John R.|title=RhoGDI: multiple functions in the regulation of Rho family GTPase activities|journal=Biochemical Journal|date=NaN undefined NaN|volume=390|issue=1|pages=1|doi=10.1042/BJ20050104}}</ref> <ref>{{cite journal|last=Garcia-Mata|first=Rafael|coauthors=Boulter, Etienne; Burridge, Keith|title=The 'invisible hand': regulation of RHO GTPases by RHOGDIs|journal=Nature Reviews Molecular Cell Biology|date=NaN undefined NaN|volume=12|issue=8|pages=493–504|doi=10.1038/nrm3153}}</ref> RhoGDI2 was initially believed to be expressed specifically in blood forming cells <ref>{{cite journal|last=Scherle|first=P|coauthors=Behrens, T; Staudt, LM|title=Ly-GDI, a GDP-dissociation inhibitor of the RhoA GTP-binding protein, is expressed preferentially in lymphocytes.|journal=Proceedings of the National Academy of Sciences of the United States of America|date=1993 Aug 15|volume=90|issue=16|pages=7568-72|pmid=8356058}}</ref> , but has subsequently been found to be highly expressed in a variety of other cell types as well <ref>{{cite journal|last=Theodorescu|first=D.|title=Reduced Expression of Metastasis Suppressor RhoGDI2 Is Associated with Decreased Survival for Patients with Bladder Cancer|journal=Clinical Cancer Research|date=1 June 2004|volume=10|issue=11|pages=3800–3806|doi=10.1158/1078-0432.CCR-03-0653}}</ref> . RhoGDI3 is predominantly expressed in brain, lung, kidney, testis and pancreas <ref>{{cite journal|last=Adra|first=CN|coauthors=Manor, D; Ko, JL; Zhu, S; Horiuchi, T; Van Aelst, L; Cerione, RA; Lim, B|title=RhoGDIgamma: a GDP-dissociation inhibitor for Rho proteins with preferential expression in brain and pancreas.|journal=Proceedings of the National Academy of Sciences of the United States of America|date=1997 Apr 29|volume=94|issue=9|pages=4279-84|pmid=9113980}}</ref> <ref>{{cite journal|last=Zalcman|first=G|coauthors=Closson, V; Camonis, J; Honoré, N; Rousseau-Merck, MF; Tavitian, A; Olofsson, B|title=RhoGDI-3 is a new GDP dissociation inhibitor (GDI). Identification of a non-cytosolic GDI protein interacting with the small GTP-binding proteins RhoB and RhoG.|journal=The Journal of biological chemistry|date=1996 Nov 29|volume=271|issue=48|pages=30366-74|pmid=8939998}}</ref> , and is targeted to specific parts of the cell such as the Golgi where it may play a role in transport or proteins in cells. <ref>{{cite journal|last=Brunet|first=N|coauthors=Morin, A; Olofsson, B|title=RhoGDI-3 regulates RhoG and targets this protein to the Golgi complex through its unique N-terminal domain.|journal=Traffic (Copenhagen, Denmark)|date=2002 May|volume=3|issue=5|pages=342-57|pmid=11967128}}</ref> <ref>{{cite journal|last=Dransart|first=E|coauthors=Morin, A; Cherfils, J; Olofsson, B|title=Uncoupling of inhibitory and shuttling functions of rho GDP dissociation inhibitors.|journal=The Journal of biological chemistry|date=2005 Feb 11|volume=280|issue=6|pages=4674-83|pmid=15513926}}</ref>.

== Disease involvement ==
Despite a high degree of sequence similarity, RhoGDI1 and RhoGDI2 are very different in their binding affinities for specific [[GTPases]] <ref>{{cite journal|last=Gorvel|first=JP|coauthors=Chang, TC; Boretto, J; Azuma, T; Chavrier, P|title=Differential properties of D4/LyGDI versus RhoGDI: phosphorylation and rho GTPase selectivity.|journal=FEBS letters|date=1998 Jan 30|volume=422|issue=2|pages=269-73|pmid=9490022}}</ref> , and more importantly, in their roles in tumor formation and spread of tumor to other organs (the process of [[Metastasis|metastasis]] ) <ref>{{cite journal|last=Harding|first=MA|coauthors=Theodorescu, D|title=RhoGDI signaling provides targets for cancer therapy.|journal=European journal of cancer (Oxford, England : 1990)|date=2010 May|volume=46|issue=7|pages=1252-9|pmid=20347589}}</ref>. For example, RhoGDI2 functions as a suppressor of metastasis but not a tumor suppressor in bladder cancer cells <ref>{{cite journal|last=Theodorescu|first=D.|title=Reduced Expression of Metastasis Suppressor RhoGDI2 Is Associated with Decreased Survival for Patients with Bladder Cancer|journal=Clinical Cancer Research|date=1 June 2004|volume=10|issue=11|pages=3800–3806|doi=10.1158/1078-0432.CCR-03-0653}}</ref><ref>{{cite journal|last=Gildea|first=JJ|coauthors=Seraj, MJ; Oxford, G; Harding, MA; Hampton, GM; Moskaluk, CA; Frierson, HF; Conaway, MR; Theodorescu, D|title=RhoGDI2 is an invasion and metastasis suppressor gene in human cancer.|journal=Cancer research|date=2002 Nov 15|volume=62|issue=22|pages=6418-23|pmid=12438227}}</ref>, while RhoGDI1 is a ubiquitous suppressor of tumor growth in all sites so far examined in bladder cancer models)<ref>{{cite journal|last=Moissoglu|first=K|coauthors=McRoberts, KS; Meier, JA; Theodorescu, D; Schwartz, MA|title=Rho GDP dissociation inhibitor 2 suppresses metastasis via unconventional regulation of RhoGTPases.|journal=Cancer research|date=2009 Apr 1|volume=69|issue=7|pages=2838-44|pmid=19276387}}</ref> , suggesting that their cellular functions must diverge to cause these differential effects.
While there are clear links between the alteration of RhoGDI2 protein levels and disease progression and/or metastasis in several types of cancer, the mechanistic underpinnings of the mode of RhoGDI2 action under carcinogenic cellular conditions are only now beginning to be understood. Evidence demonstrates that RhoGDI2 inhibits the endothelin axis (15) and crosstalk with macrophages within the micrometastatic microenvironment to inhibit metastatic outgrowth<ref>{{cite journal|last=Said|first=Neveen|coauthors=Smith, Steven; Sanchez-Carbayo, Marta; Theodorescu, Dan|title=Tumor endothelin-1 enhances metastatic colonization of the lung in mouse xenograft models of bladder cancer|journal=Journal of Clinical Investigation|date=NaN undefined NaN|volume=121|issue=1|pages=132–147|doi=10.1172/JCI42912}}</ref>. As such, RhoGDI2 could prove important in the regulation of tumor dormancy. Targeting this axis with orally available endothelin receptor antagonists<ref>{{cite journal|last=Nelson|first=J|coauthors=Bagnato, A; Battistini, B; Nisen, P|title=The endothelin axis: emerging role in cancer.|journal=Nature reviews. Cancer|date=2003 Feb|volume=3|issue=2|pages=110-6|pmid=12563310}}</ref> may prove efficacious in mimicking the inhibitory role of RhoGDI2 by preventing macrophage infiltration into the micrometastatic niche <ref>{{cite journal|last=Said|first=Neveen|coauthors=Sanchez-Carbayo, Marta; Smith, Steven C.; Theodorescu, Dan|title=RhoGDI2 suppresses lung metastasis in mice by reducing tumor versican expression and macrophage infiltration|journal=Journal of Clinical Investigation|date=NaN undefined NaN|volume=122|issue=4|pages=1503–1518|doi=10.1172/JCI61392}}</ref>. Recent work has also determined that genetic and pharmacologic targeting of [[CCL2|Chemokine (C-C motif) ligand 2 (CCL2)]] also known as monocyte chemotactic protein-1 (MCP-1) or small inducible cytokine A2 , its receptor CCR2 and pharmacologic ablation of macrophages can also phenocopy the effect of RhoGDI2 expression to prevent metastatic colonization of the lung67 and that RhoGDI2 is suppressor of versican, a protein that has been shown to promote cell migration<ref>{{cite journal|last=Wu|first=Y|coauthors=Siadaty, MS; Berens, ME; Hampton, GM; Theodorescu, D|title=Overlapping gene expression profiles of cell migration and tumor invasion in human bladder cancer identify metallothionein 1E and nicotinamide N-methyltransferase as novel regulators of cell migration.|journal=Oncogene|date=2008 Nov 6|volume=27|issue=52|pages=6679-89|pmid=18724390}}</ref> and metastasis in several tumor models.

In contrast to its role as a metastasis suppressor in bladder cancer, in breast, RhoGDI2 expression has been reported to be upregulated in cancer <ref>{{cite journal|last=Moon|first=HG|coauthors=Jeong, SH; Ju, YT; Jeong, CY; Lee, JS; Lee, YJ; Hong, SC; Choi, SK; Ha, WS; Park, ST; Jung, EJ|title=Up-regulation of RhoGDI2 in human breast cancer and its prognostic implications.|journal=Cancer research and treatment : official journal of Korean Cancer Association|date=2010 Sep|volume=42|issue=3|pages=151-6|pmid=20948920}}</ref> and to promote invasion of breast cancer cells <ref>{{cite journal|last=Zhang|first=Y|coauthors=Zhang, B|title=D4-GDI, a Rho GTPase regulator, promotes breast cancer cell invasiveness.|journal=Cancer research|date=2006 Jun 1|volume=66|issue=11|pages=5592-8|pmid=16740694}}</ref> , while another report found a biphasic expression pattern of RhoGDI2 in breast cancer with decreased expression correlating with lymph node metastasis <ref>{{cite journal|last=Hu|first=LD|coauthors=Zou, HF; Zhan, SX; Cao, KM|title=Biphasic expression of RhoGDI2 in the progression of breast cancer and its negative relation with lymph node metastasis.|journal=Oncology reports|date=2007 Jun|volume=17|issue=6|pages=1383-9|pmid=17487395}}</ref> .


==References==
==References==

Revision as of 14:35, 8 August 2012

Template:PBB Rho GDP-dissociation inhibitor 2 is a protein that in humans is encoded by the ARHGDIB gene.[1][2][3]. Aliases of this gene include RhoGDI2, GDID4, Rho GDI 2, and others [4].

Template:PBB Summary

Interactions

ARHGDIB has been shown to interact with VAV1[5] and Src.[6]

Gene Family

RhoGDI2 (ARHGDIB) is part of a family of three members: RhoGDI1, RhoGDI2 (also known as RhoGDIB, D4-GDI or Ly-GDI) and RhoGDI3. RhoGDI1 is expressed in many organs and is the best studied member of the family.[7] [8] [9] RhoGDI2 was initially believed to be expressed specifically in blood forming cells [10] , but has subsequently been found to be highly expressed in a variety of other cell types as well [11] . RhoGDI3 is predominantly expressed in brain, lung, kidney, testis and pancreas [12] [13] , and is targeted to specific parts of the cell such as the Golgi where it may play a role in transport or proteins in cells. [14] [15].

Disease involvement

Despite a high degree of sequence similarity, RhoGDI1 and RhoGDI2 are very different in their binding affinities for specific GTPases [16] , and more importantly, in their roles in tumor formation and spread of tumor to other organs (the process of metastasis ) [17]. For example, RhoGDI2 functions as a suppressor of metastasis but not a tumor suppressor in bladder cancer cells [18][19], while RhoGDI1 is a ubiquitous suppressor of tumor growth in all sites so far examined in bladder cancer models)[20] , suggesting that their cellular functions must diverge to cause these differential effects. While there are clear links between the alteration of RhoGDI2 protein levels and disease progression and/or metastasis in several types of cancer, the mechanistic underpinnings of the mode of RhoGDI2 action under carcinogenic cellular conditions are only now beginning to be understood. Evidence demonstrates that RhoGDI2 inhibits the endothelin axis (15) and crosstalk with macrophages within the micrometastatic microenvironment to inhibit metastatic outgrowth[21]. As such, RhoGDI2 could prove important in the regulation of tumor dormancy. Targeting this axis with orally available endothelin receptor antagonists[22] may prove efficacious in mimicking the inhibitory role of RhoGDI2 by preventing macrophage infiltration into the micrometastatic niche [23]. Recent work has also determined that genetic and pharmacologic targeting of Chemokine (C-C motif) ligand 2 (CCL2) also known as monocyte chemotactic protein-1 (MCP-1) or small inducible cytokine A2 , its receptor CCR2 and pharmacologic ablation of macrophages can also phenocopy the effect of RhoGDI2 expression to prevent metastatic colonization of the lung67 and that RhoGDI2 is suppressor of versican, a protein that has been shown to promote cell migration[24] and metastasis in several tumor models.

In contrast to its role as a metastasis suppressor in bladder cancer, in breast, RhoGDI2 expression has been reported to be upregulated in cancer [25] and to promote invasion of breast cancer cells [26] , while another report found a biphasic expression pattern of RhoGDI2 in breast cancer with decreased expression correlating with lymph node metastasis [27] .

References

  1. ^ Lelias JM, Adra CN, Wulf GM, Guillemot JC, Khagad M, Caput D, Lim B (1993). "cDNA cloning of a human mRNA preferentially expressed in hematopoietic cells and with homology to a GDP-dissociation inhibitor for the rho GTP-binding proteins". Proc Natl Acad Sci U S A. 90 (4): 1479–83. doi:10.1073/pnas.90.4.1479. PMC 45897. PMID 8434008. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
  2. ^ Scherle P, Behrens T, Staudt LM (1993). "Ly-GDI, a GDP-dissociation inhibitor of the RhoA GTP-binding protein, is expressed preferentially in lymphocytes". Proc Natl Acad Sci U S A. 90 (16): 7568–72. doi:10.1073/pnas.90.16.7568. PMC 47183. PMID 8356058. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
  3. ^ "Entrez Gene: ARHGDIB Rho GDP dissociation inhibitor (GDI) beta".
  4. ^ ""Gene Cards: ARHGDIB".
  5. ^ Groysman, M (2000). "Vav, a GDP/GTP nucleotide exchange factor, interacts with GDIs, proteins that inhibit GDP/GTP dissociation". FEBS Lett. 467 (1). NETHERLANDS: 75–80. doi:10.1016/S0014-5793(00)01121-2. ISSN 0014-5793. PMID 10664460. {{cite journal}}: Cite has empty unknown parameters: |laydate=, |laysummary=, and |laysource= (help); Unknown parameter |coauthors= ignored (|author= suggested) (help); Unknown parameter |month= ignored (help)
  6. ^ Wu, Y. (25 March 2009). "Src phosphorylation of RhoGDI2 regulates its metastasis suppressor function". Proceedings of the National Academy of Sciences. 106 (14): 5807–5812. doi:10.1073/pnas.0810094106. {{cite journal}}: Unknown parameter |coauthors= ignored (|author= suggested) (help)
  7. ^ DerMardirossian, Céline (NaN undefined NaN). "GDIs: central regulatory molecules in Rho GTPase activation". Trends in Cell Biology. 15 (7): 356–363. doi:doi:10.1016/j.tcb.2005.05.001. {{cite journal}}: Check |doi= value (help); Check date values in: |date= (help); Unknown parameter |coauthors= ignored (|author= suggested) (help)
  8. ^ Dovas, Athanassios (NaN undefined NaN). "RhoGDI: multiple functions in the regulation of Rho family GTPase activities". Biochemical Journal. 390 (1): 1. doi:10.1042/BJ20050104. {{cite journal}}: Check date values in: |date= (help); Unknown parameter |coauthors= ignored (|author= suggested) (help); no-break space character in |coauthors= at position 15 (help)
  9. ^ Garcia-Mata, Rafael (NaN undefined NaN). "The 'invisible hand': regulation of RHO GTPases by RHOGDIs". Nature Reviews Molecular Cell Biology. 12 (8): 493–504. doi:10.1038/nrm3153. {{cite journal}}: Check date values in: |date= (help); Unknown parameter |coauthors= ignored (|author= suggested) (help)
  10. ^ Scherle, P (1993 Aug 15). "Ly-GDI, a GDP-dissociation inhibitor of the RhoA GTP-binding protein, is expressed preferentially in lymphocytes". Proceedings of the National Academy of Sciences of the United States of America. 90 (16): 7568–72. PMID 8356058. {{cite journal}}: Check date values in: |date= (help); Unknown parameter |coauthors= ignored (|author= suggested) (help)
  11. ^ Theodorescu, D. (1 June 2004). "Reduced Expression of Metastasis Suppressor RhoGDI2 Is Associated with Decreased Survival for Patients with Bladder Cancer". Clinical Cancer Research. 10 (11): 3800–3806. doi:10.1158/1078-0432.CCR-03-0653.
  12. ^ Adra, CN (1997 Apr 29). "RhoGDIgamma: a GDP-dissociation inhibitor for Rho proteins with preferential expression in brain and pancreas". Proceedings of the National Academy of Sciences of the United States of America. 94 (9): 4279–84. PMID 9113980. {{cite journal}}: Check date values in: |date= (help); Unknown parameter |coauthors= ignored (|author= suggested) (help)
  13. ^ Zalcman, G (1996 Nov 29). "RhoGDI-3 is a new GDP dissociation inhibitor (GDI). Identification of a non-cytosolic GDI protein interacting with the small GTP-binding proteins RhoB and RhoG". The Journal of biological chemistry. 271 (48): 30366–74. PMID 8939998. {{cite journal}}: Check date values in: |date= (help); Unknown parameter |coauthors= ignored (|author= suggested) (help)
  14. ^ Brunet, N (2002 May). "RhoGDI-3 regulates RhoG and targets this protein to the Golgi complex through its unique N-terminal domain". Traffic (Copenhagen, Denmark). 3 (5): 342–57. PMID 11967128. {{cite journal}}: Check date values in: |date= (help); Unknown parameter |coauthors= ignored (|author= suggested) (help)
  15. ^ Dransart, E (2005 Feb 11). "Uncoupling of inhibitory and shuttling functions of rho GDP dissociation inhibitors". The Journal of biological chemistry. 280 (6): 4674–83. PMID 15513926. {{cite journal}}: Check date values in: |date= (help); Unknown parameter |coauthors= ignored (|author= suggested) (help)
  16. ^ Gorvel, JP (1998 Jan 30). "Differential properties of D4/LyGDI versus RhoGDI: phosphorylation and rho GTPase selectivity". FEBS letters. 422 (2): 269–73. PMID 9490022. {{cite journal}}: Check date values in: |date= (help); Unknown parameter |coauthors= ignored (|author= suggested) (help)
  17. ^ Harding, MA (2010 May). "RhoGDI signaling provides targets for cancer therapy". European journal of cancer (Oxford, England : 1990). 46 (7): 1252–9. PMID 20347589. {{cite journal}}: Check date values in: |date= (help); Unknown parameter |coauthors= ignored (|author= suggested) (help)
  18. ^ Theodorescu, D. (1 June 2004). "Reduced Expression of Metastasis Suppressor RhoGDI2 Is Associated with Decreased Survival for Patients with Bladder Cancer". Clinical Cancer Research. 10 (11): 3800–3806. doi:10.1158/1078-0432.CCR-03-0653.
  19. ^ Gildea, JJ (2002 Nov 15). "RhoGDI2 is an invasion and metastasis suppressor gene in human cancer". Cancer research. 62 (22): 6418–23. PMID 12438227. {{cite journal}}: Check date values in: |date= (help); Unknown parameter |coauthors= ignored (|author= suggested) (help)
  20. ^ Moissoglu, K (2009 Apr 1). "Rho GDP dissociation inhibitor 2 suppresses metastasis via unconventional regulation of RhoGTPases". Cancer research. 69 (7): 2838–44. PMID 19276387. {{cite journal}}: Check date values in: |date= (help); Unknown parameter |coauthors= ignored (|author= suggested) (help)
  21. ^ Said, Neveen (NaN undefined NaN). "Tumor endothelin-1 enhances metastatic colonization of the lung in mouse xenograft models of bladder cancer". Journal of Clinical Investigation. 121 (1): 132–147. doi:10.1172/JCI42912. {{cite journal}}: Check date values in: |date= (help); Unknown parameter |coauthors= ignored (|author= suggested) (help)
  22. ^ Nelson, J (2003 Feb). "The endothelin axis: emerging role in cancer". Nature reviews. Cancer. 3 (2): 110–6. PMID 12563310. {{cite journal}}: Check date values in: |date= (help); Unknown parameter |coauthors= ignored (|author= suggested) (help)
  23. ^ Said, Neveen (NaN undefined NaN). "RhoGDI2 suppresses lung metastasis in mice by reducing tumor versican expression and macrophage infiltration". Journal of Clinical Investigation. 122 (4): 1503–1518. doi:10.1172/JCI61392. {{cite journal}}: Check date values in: |date= (help); Unknown parameter |coauthors= ignored (|author= suggested) (help)
  24. ^ Wu, Y (2008 Nov 6). "Overlapping gene expression profiles of cell migration and tumor invasion in human bladder cancer identify metallothionein 1E and nicotinamide N-methyltransferase as novel regulators of cell migration". Oncogene. 27 (52): 6679–89. PMID 18724390. {{cite journal}}: Check date values in: |date= (help); Unknown parameter |coauthors= ignored (|author= suggested) (help)
  25. ^ Moon, HG (2010 Sep). "Up-regulation of RhoGDI2 in human breast cancer and its prognostic implications". Cancer research and treatment : official journal of Korean Cancer Association. 42 (3): 151–6. PMID 20948920. {{cite journal}}: Check date values in: |date= (help); Unknown parameter |coauthors= ignored (|author= suggested) (help)
  26. ^ Zhang, Y (2006 Jun 1). "D4-GDI, a Rho GTPase regulator, promotes breast cancer cell invasiveness". Cancer research. 66 (11): 5592–8. PMID 16740694. {{cite journal}}: Check date values in: |date= (help); Unknown parameter |coauthors= ignored (|author= suggested) (help)
  27. ^ Hu, LD (2007 Jun). "Biphasic expression of RhoGDI2 in the progression of breast cancer and its negative relation with lymph node metastasis". Oncology reports. 17 (6): 1383–9. PMID 17487395. {{cite journal}}: Check date values in: |date= (help); Unknown parameter |coauthors= ignored (|author= suggested) (help)

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