A new phosphatidylinositol 4,5-bisphosphate-binding site located in the C2 domain of protein kinase Calpha. (Q40690959)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12426311%20AND%20SRC:MED&resulttype=core&format=json

14 December 2019

title

A new phosphatidylinositol 4,5-bisphosphate-binding site located in the C2 domain of protein kinase Calpha (English)

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14 December 2019

1

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14 December 2019

Juan C. Gómez-Fernández

series ordinal

4

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14 December 2019

author name string

Josefa García-García

series ordinal

2

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14 December 2019

José A Rodríguez-Alfaro

series ordinal

3

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14 December 2019

language of work or name

English

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publication date

7 November 2002

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Journal of Biological Chemistry

14 December 2019

published in

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14 December 2019

volume

278

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14 December 2019

issue

7

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14 December 2019

page(s)

4972-4980

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The synthesis and cellular roles of phosphatidylinositol 4,5-bisphosphate

14 December 2019

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Lipid structure and not membrane structure is the major determinant in the regulation of protein kinase C by phosphatidylserine.

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Additional binding sites for anionic phospholipids and calcium ions in the crystal structures of complexes of the C2 domain of protein kinase calpha.

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Ca(2+) bridges the C2 membrane-binding domain of protein kinase Calpha directly to phosphatidylserine

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Phosphatidylinositol 4-phosphate 5-kinase alpha is a downstream effector of the small G protein ARF6 in membrane ruffle formation

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