NCS-1 inhibits insulin-stimulated GLUT4 translocation in 3T3L1 adipocytes through a phosphatidylinositol 4-kinase-dependent pathway. (Q34128449)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12011096%20AND%20SRC:MED&resulttype=core&format=json

8 November 2019

title

NCS-1 inhibits insulin-stimulated GLUT4 translocation in 3T3L1 adipocytes through a phosphatidylinositol 4-kinase-dependent pathway (English)

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8 November 2019

1 reference

1 reference

1

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8 November 2019

Andrew F Russo

4

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8 November 2019

author name string

Paul L Durham

2

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8 November 2019

Jeffery R Smith

3

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8 November 2019

Andreas Jeromin

5

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8 November 2019

Jeffrey E Pessin

6

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8 November 2019

language of work or name

English

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publication date

13 May 2002

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Journal of Biological Chemistry

8 November 2019

number of pages

7

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based on heuristic

inferred from page(s)

published in

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8 November 2019

volume

277

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8 November 2019

issue

30

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8 November 2019

page(s)

27494-27500

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Turned on by Ca2+! The physiology and pathology of Ca(2+)-binding proteins in the retina

8 November 2019

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Phosphatidylinositol 4-kinase, but not phosphatidylinositol 3-kinase, is present in GLUT4-containing vesicles isolated from rat skeletal muscle

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Regulation of insulin-stimulated GLUT4 translocation by Munc18c in 3T3L1 adipocytes

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Chelation of intracellular calcium prevents stimulation of glucose transport by insulin and insulinomimetic agents in the adipocyte. Evidence for a common mechanism

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Calmodulin antagonists inhibit insulin-stimulated GLUT4 (glucose transporter 4) translocation by preventing the formation of phosphatidylinositol 3,4,5-trisphosphate in 3T3L1 adipocytes

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Endothelin stimulates glucose uptake and GLUT4 translocation via activation of endothelin ETA receptor in 3T3-L1 adipocytes

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Endothelin-1-induced GLUT4 translocation is mediated via Galpha(q/11) protein and phosphatidylinositol 3-kinase in 3T3-L1 adipocytes

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Insulin-stimulated GLUT4 translocation requires the CAP-dependent activation of TC10

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