Jump to content

ACVR2A: Difference between revisions

From Wikipedia, the free encyclopedia
Browse history interactively
← Previous editNext edit →
Content deleted Content added
VisualWikitext
removed no longer needed PBB controls and templates; consistent ref formatting; wikify
m →Interactions: Added 1 doi to a journal cite using AWB (10210)
Line 11: Line 11:


ACVR2A has been shown to [[Protein-protein interaction|interact]] with:
ACVR2A has been shown to [[Protein-protein interaction|interact]] with:
* [[ACVR1B]],<ref name = pmid9892009>{{cite journal | date = January 1999 | author = Lebrun JJ, Takabe K, Chen Y, Vale W | title = Roles of pathway-specific and inhibitory Smads in activin receptor signaling | journal = Mol. Endocrinol. | volume = 13 | issue = 1 | pages = 15-23 | pmid = 9892009 | doi = 10.1210/mend.13.1.0218}}</ref><ref name = pmid8612709>{{cite journal | date = May 1996 | author = De Winter JP, De Vries CJ, Van Achterberg TA, Ameerun RF, Feijen A, Sugino H, De Waele P, Huylebroeck D, Verschueren K, Van Den Eijden-Van Raaij AJ | title = Truncated activin type II receptors inhibit bioactivity by the formation of heteromeric complexes with activin type I. receptors | journal = Exp. Cell Res. | volume = 224 | issue = 2 | pages = 323-34 | pmid = 8612709 | doi = }}</ref>
* [[ACVR1B]],<ref name = pmid9892009>{{cite journal | date = January 1999 | author = Lebrun JJ, Takabe K, Chen Y, Vale W | title = Roles of pathway-specific and inhibitory Smads in activin receptor signaling | journal = Mol. Endocrinol. | volume = 13 | issue = 1 | pages = 15-23 | pmid = 9892009 | doi = 10.1210/mend.13.1.0218}}</ref><ref name = pmid8612709>{{cite journal | date = May 1996 | author = De Winter JP, De Vries CJ, Van Achterberg TA, Ameerun RF, Feijen A, Sugino H, De Waele P, Huylebroeck D, Verschueren K, Van Den Eijden-Van Raaij AJ | title = Truncated activin type II receptors inhibit bioactivity by the formation of heteromeric complexes with activin type I. receptors | journal = Exp. Cell Res. | volume = 224 | issue = 2 | pages = 323-34 | pmid = 8612709 | doi = 10.1006/excr.1996.0142}}</ref>
* [[INHBA]],<ref name = pmid10746731>{{cite journal | date = March 2000 | author = Lewis KA, Gray PC, Blount AL, MacConell LA, Wiater E, Bilezikjian LM, Vale W | title = Betaglycan binds inhibin and can mediate functional antagonism of activin signalling | journal = Nature | volume = 404 | issue = 6776 | pages = 411-4 | pmid = 10746731 | doi = 10.1038/35006129}}</ref><ref name = pmid9202237>{{cite journal | date = July 1997 | author = Martens JW, de Winter JP, Timmerman MA, McLuskey A, van Schaik RH, Themmen AP, de Jong FH | title = Inhibin interferes with activin signaling at the level of the activin receptor complex in Chinese hamster ovary cells | journal = Endocrinology | volume = 138 | issue = 7 | pages = 2928-36 | pmid = 9202237 | doi = 10.1210/endo.138.7.5250}}</ref> and
* [[INHBA]],<ref name = pmid10746731>{{cite journal | date = March 2000 | author = Lewis KA, Gray PC, Blount AL, MacConell LA, Wiater E, Bilezikjian LM, Vale W | title = Betaglycan binds inhibin and can mediate functional antagonism of activin signalling | journal = Nature | volume = 404 | issue = 6776 | pages = 411-4 | pmid = 10746731 | doi = 10.1038/35006129}}</ref><ref name = pmid9202237>{{cite journal | date = July 1997 | author = Martens JW, de Winter JP, Timmerman MA, McLuskey A, van Schaik RH, Themmen AP, de Jong FH | title = Inhibin interferes with activin signaling at the level of the activin receptor complex in Chinese hamster ovary cells | journal = Endocrinology | volume = 138 | issue = 7 | pages = 2928-36 | pmid = 9202237 | doi = 10.1210/endo.138.7.5250}}</ref> and
* [[SYNJ2BP]].<ref name = pmid15451561>{{cite journal | date = October 2004 | author = Tsuchida K, Nakatani M, Matsuzaki T, Yamakawa N, Liu Z, Bao Y, Arai KY, Murakami T, Takehara Y, Kurisaki A, Sugino H | title = Novel factors in regulation of activin signaling | journal = Mol. Cell. Endocrinol. | volume = 225 | issue = 1-2 | pages = 1-8 | pmid = 15451561 | doi = 10.1016/j.mce.2004.02.006}}</ref><ref name = pmid11882656>{{cite journal | date = May 2002 | author = Matsuzaki T, Hanai S, Kishi H, Liu Z, Bao Y, Kikuchi A, Tsuchida K, Sugino H | title = Regulation of endocytosis of activin type II receptors by a novel PDZ protein through Ral/Ral-binding protein 1-dependent pathway | journal = J. Biol. Chem. | volume = 277 | issue = 21 | pages = 19008-18 | pmid = 11882656 | doi = 10.1074/jbc.M112472200}}</ref>
* [[SYNJ2BP]].<ref name = pmid15451561>{{cite journal | date = October 2004 | author = Tsuchida K, Nakatani M, Matsuzaki T, Yamakawa N, Liu Z, Bao Y, Arai KY, Murakami T, Takehara Y, Kurisaki A, Sugino H | title = Novel factors in regulation of activin signaling | journal = Mol. Cell. Endocrinol. | volume = 225 | issue = 1-2 | pages = 1-8 | pmid = 15451561 | doi = 10.1016/j.mce.2004.02.006}}</ref><ref name = pmid11882656>{{cite journal | date = May 2002 | author = Matsuzaki T, Hanai S, Kishi H, Liu Z, Bao Y, Kikuchi A, Tsuchida K, Sugino H | title = Regulation of endocytosis of activin type II receptors by a novel PDZ protein through Ral/Ral-binding protein 1-dependent pathway | journal = J. Biol. Chem. | volume = 277 | issue = 21 | pages = 19008-18 | pmid = 11882656 | doi = 10.1074/jbc.M112472200}}</ref>

Revision as of 10:14, 24 May 2014

Template:PBB

Activin receptor type-2A is a protein that in humans is encoded by the ACVR2A gene.[1][2][3] ACVR2A is an activin type 2 receptor.

Function

This gene encodes activin A type II receptor. Activins are dimeric growth and differentiation factors which belong to the transforming growth factor-beta (TGF-beta) superfamily of structurally related signaling proteins. Activins signal through a heteromeric complex of receptor serine kinases which include at least two type I (I and IB) and two type II (II and IIB) receptors. These receptors are all transmembrane proteins, composed of a ligand-binding extracellular domain with cysteine-rich region, a transmembrane domain, and a cytoplasmic domain with predicted serine/threonine specificity. Type I receptors are essential for signaling; and type II receptors are required for binding ligands and for expression of type I receptors. Type I and II receptors form a stable complex after ligand binding, resulting in phosphorylation of type I receptors by type II receptors. Type II receptors are considered to be constitutively active kinases.[3]

Interactions

ACVR2A has been shown to interact with:


References

  1. ^ Donaldson CJ, Mathews LS, Vale WW (May 1992). "Molecular cloning and binding properties of the human type II activin receptor". Biochem Biophys Res Commun. 184 (1): 310–316. doi:10.1016/0006-291X(92)91194-U. PMID 1314589.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  2. ^ Bondestam J, Horelli-Kuitunen N, Hilden K, Ritvos O, Aaltonen J (April 2000). "Assignment of ACVR2 and ACVR2B the human activin receptor type II and IIB genes to chromosome bands 2q22.2→q23.3 and 3p22 and the human follistatin gene (FST) to chromosome 5q11.2 by FISH". Cytogenet Cell Genet. 87 (3–4): 219–220. doi:10.1159/000015429. PMID 10702675.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  3. ^ a b "Entrez Gene: ACVR2A activin A receptor, type IIA".
  4. ^ Lebrun JJ, Takabe K, Chen Y, Vale W (January 1999). "Roles of pathway-specific and inhibitory Smads in activin receptor signaling". Mol. Endocrinol. 13 (1): 15–23. doi:10.1210/mend.13.1.0218. PMID 9892009.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  5. ^ De Winter JP, De Vries CJ, Van Achterberg TA, Ameerun RF, Feijen A, Sugino H, De Waele P, Huylebroeck D, Verschueren K, Van Den Eijden-Van Raaij AJ (May 1996). "Truncated activin type II receptors inhibit bioactivity by the formation of heteromeric complexes with activin type I. receptors". Exp. Cell Res. 224 (2): 323–34. doi:10.1006/excr.1996.0142. PMID 8612709.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  6. ^ Lewis KA, Gray PC, Blount AL, MacConell LA, Wiater E, Bilezikjian LM, Vale W (March 2000). "Betaglycan binds inhibin and can mediate functional antagonism of activin signalling". Nature. 404 (6776): 411–4. doi:10.1038/35006129. PMID 10746731.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  7. ^ Martens JW, de Winter JP, Timmerman MA, McLuskey A, van Schaik RH, Themmen AP, de Jong FH (July 1997). "Inhibin interferes with activin signaling at the level of the activin receptor complex in Chinese hamster ovary cells". Endocrinology. 138 (7): 2928–36. doi:10.1210/endo.138.7.5250. PMID 9202237.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  8. ^ Tsuchida K, Nakatani M, Matsuzaki T, Yamakawa N, Liu Z, Bao Y, Arai KY, Murakami T, Takehara Y, Kurisaki A, Sugino H (October 2004). "Novel factors in regulation of activin signaling". Mol. Cell. Endocrinol. 225 (1–2): 1–8. doi:10.1016/j.mce.2004.02.006. PMID 15451561.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  9. ^ Matsuzaki T, Hanai S, Kishi H, Liu Z, Bao Y, Kikuchi A, Tsuchida K, Sugino H (May 2002). "Regulation of endocytosis of activin type II receptors by a novel PDZ protein through Ral/Ral-binding protein 1-dependent pathway". J. Biol. Chem. 277 (21): 19008–18. doi:10.1074/jbc.M112472200. PMID 11882656.{{cite journal}}: CS1 maint: multiple names: authors list (link) CS1 maint: unflagged free DOI (link)

Further reading


Stub icon

This genetics article is a stub. You can help Wikipedia by expanding it.

Retrieved from "https://en.wikipedia.org/w/index.php?title=ACVR2A&oldid=609926026"