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Article

Calmodulin binds to the Rab GTPase activating protein required for insulin-stimulated GLUT4 translocation.

Biochemical and biophysical research communications - 16 Sept 2005

Kane Susan, Lienhard Gustav E

Abstract excerpt

Recently, we described a 160 kDa protein with a Rab GTPase activating protein domain that is phosphorylated on multiple sites by the protein kinase Akt (designated AS160). Phosphorylation of AS160 in adipocytes is required for insulin-stimulated translocation of the glucose transporter GLUT4 to the plasma membrane. In the present study, we searched for proteins that interact with the GTPase activating protein...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 16055084
DOI: 10.1016/j.bbrc.2005.07.056

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Calmodulin binds to the Rab GTPase activating protein required for insulin-stimulated GLUT4 translocation.PMID 16055084Read ↗

Insulin-stimulated phosphorylation of a Rab GTPase-activating protein regulates GLUT4 translocation.Semantic proximity Read ↗

Complementary regulation of TBC1D1 and AS160 by growth factors, insulin and AMPK activators.Semantic proximity Read ↗

A method to identify serine kinase substrates. Akt phosphorylates a novel adipocyte protein with a Rab GTPase-activating protein (GAP) domain.Semantic proximity Read ↗

Mice with AS160/TBC1D4-Thr649Ala knockin mutation are glucose intolerant with reduced insulin sensitivity and altered GLUT4 trafficking.Semantic proximity Read ↗

The Inactivation of RabGAP Function of AS160 Promotes Lysosomal Degradation of GLUT4 and Causes Postprandial Hyperglycemia and Hyperinsulinemia.Semantic proximity Read ↗

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Functional consequence of targeting protein kinase B/Akt to GLUT4 vesicles.Semantic proximity Read ↗

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