Lipid raft disruption triggers protein kinase C and Src-dependent protein kinase D activation and Kidins220 phosphorylation in neuronal cells (Q44851101)

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scientific article published on 19 April 2004

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English	Lipid raft disruption triggers protein kinase C and Src-dependent protein kinase D activation and Kidins220 phosphorylation in neuronal cells	scientific article published on 19 April 2004

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

6 December 2017

Lipid raft disruption triggers protein kinase C and Src-dependent protein kinase D activation and Kidins220 phosphorylation in neuronal cells (English)

1 reference

Europe PubMed Central

PubMed publication ID

6 December 2017

phosphorylation

1 reference

based on heuristic

inferred from title

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based on heuristic

inferred from title

author name string

Noemí Cabrera-Poch

1

1 reference

Europe PubMed Central

PubMed publication ID

6 December 2017

Lucía Sánchez-Ruiloba

2

1 reference

Europe PubMed Central

PubMed publication ID

6 December 2017

María Rodríguez-Martínez

3

1 reference

Europe PubMed Central

PubMed publication ID

6 December 2017

Teresa Iglesias

4

1 reference

Europe PubMed Central

PubMed publication ID

6 December 2017

language of work or name

0 references

publication date

19 April 2004

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Europe PubMed Central

PubMed publication ID

6 December 2017

number of pages

11

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based on heuristic

inferred from page(s)

Journal of Biological Chemistry

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Europe PubMed Central

PubMed publication ID

6 December 2017

279

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Europe PubMed Central

PubMed publication ID

6 December 2017

27

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Europe PubMed Central

PubMed publication ID

6 December 2017

28592-28602

1 reference

Europe PubMed Central

PubMed publication ID

6 December 2017

Identification and cloning of Kidins220, a novel neuronal substrate of protein kinase D.

1 reference

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PDZ proteins organize synaptic signaling pathways

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Molecular cloning and characterization of protein kinase D: a target for diacylglycerol and phorbol esters with a distinctive catalytic domain

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Protein kinase D: an intracellular traffic regulator on the move

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Protein kinase D: a family affair

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Bombesin, vasopressin, endothelin, bradykinin, and platelet-derived growth factor rapidly activate protein kinase D through a protein kinase C-dependent signal transduction pathway.

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CCK2 (CCK(B)/gastrin) receptor mediates rapid protein kinase D (PKD) activation through a protein kinase C-dependent pathway

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Spatial and temporal regulation of protein kinase D (PKD)

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Identification of in vivo phosphorylation sites required for protein kinase D activation.

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The pleckstrin homology domain of protein kinase D interacts preferentially with the eta isoform of protein kinase C

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Activation loop Ser744 and Ser748 in protein kinase D are transphosphorylated in vivo.

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Protein kinase C phosphorylates protein kinase D activation loop Ser744 and Ser748 and releases autoinhibition by the pleckstrin homology domain.

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Oxidative stress induces protein kinase D activation in intact cells. Involvement of Src and dependence on protein kinase C.

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Tyrosine phosphorylation of protein kinase D in the pleckstrin homology domain leads to activation

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Cell-type specific phosphorylation of threonines T654 and T669 by PKD defines the signal capacity of the EGF receptor

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Protein kinase C (PKC)eta-mediated PKC mu activation modulates ERK and JNK signal pathways

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Protein kinase D complexes with C-Jun N-terminal kinase via activation loop phosphorylation and phosphorylates the C-Jun N-terminus

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Protein kinase C mu is located at the Golgi compartment

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Gbetagamma-mediated regulation of Golgi organization is through the direct activation of protein kinase D

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Protein kinase D regulates the fission of cell surface destined transport carriers from the trans-Golgi network

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Protein kinase C mu (PKC mu) associates with the B cell antigen receptor complex and regulates lymphocyte signaling

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Protein kinase D potentiates DNA synthesis and cell proliferation induced by bombesin, vasopressin, or phorbol esters in Swiss 3T3 cells

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Rapid protein kinase D translocation in response to G protein-coupled receptor activation. Dependence on protein kinase C.

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Vasopressin-induced intracellular redistribution of protein kinase D in intestinal epithelial cells

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Regulated internalization of caveolae

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Functional rafts in cell membranes

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Lipid rafts and signal transduction

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Identifiers

10.1074/JBC.M312242200

1 reference

Europe PubMed Central

PubMed publication ID

6 December 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

6 December 2017

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