RGD Reference Report - Mechanisms of biphasic insulin-granule exocytosis - roles of the cytoskeleton, small GTPases and SNARE proteins. - Rat Genome Database

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Mechanisms of biphasic insulin-granule exocytosis - roles of the cytoskeleton, small GTPases and SNARE proteins.

Authors: Wang, Z  Thurmond, DC 
Citation: Wang Z and Thurmond DC, J Cell Sci. 2009 Apr 1;122(Pt 7):893-903.
RGD ID: 2311087
Pubmed: PMID:19295123   (View Abstract at PubMed)
PMCID: PMC2720925   (View Article at PubMed Central)
DOI: DOI:10.1242/jcs.034355   (Journal Full-text)

The release of insulin from pancreatic islets requires negative regulation to ensure low levels of insulin release under resting conditions, as well as positive regulation to facilitate robust responsiveness to conditions of elevated fuel or glucose. The first phase of release involves the plasma-membrane fusion of a small pool of granules, termed the readily releasable pool; these granules are already at the membrane under basal conditions, and discharge their cargo in response to nutrient and also non-nutrient secretagogues. By contrast, second-phase secretion is evoked exclusively by nutrients, and involves the mobilization of intracellular granules to t-SNARE sites at the plasma membrane to enable the distal docking and fusion steps of insulin exocytosis. Nearly 40 years ago, the actin cytoskeleton was first recognized as a key mediator of biphasic insulin release, and was originally presumed to act as a barrier to block granule docking at the cell periphery. More recently, however, the discovery of cycling GTPases that are involved in F-actin reorganization in the islet beta-cell, combined with the availability of reagents that are more specific and tools with which to study the mechanisms that underlie granule movement, have contributed greatly to our understanding of the role of the cytoskeleton in regulating biphasic insulin secretion. Herein, we provide historical perspective and review recent progress that has been made towards integrating cytoskeletal reorganization and cycling of small Rho-, Rab- and Ras-family GTPases into our current models of stimulus-secretion coupling and second-phase insulin release.

Objects Annotated

Genes (Rattus norvegicus)
Cdc42  (cell division cycle 42)
Rab27a  (RAB27A, member RAS oncogene family)
Rab3a  (RAB3A, member RAS oncogene family)
Stx1a  (syntaxin 1A)
Stxbp1  (syntaxin binding protein 1)
Unc13a  (unc-13 homolog A)
Vamp2  (vesicle-associated membrane protein 2)

Genes (Mus musculus)
Cdc42  (cell division cycle 42)
Rab27a  (RAB27A, member RAS oncogene family)
Rab3a  (RAB3A, member RAS oncogene family)
Stx1a  (syntaxin 1A (brain))
Stxbp1  (syntaxin binding protein 1)
Unc13a  (unc-13 homolog A)
Vamp2  (vesicle-associated membrane protein 2)

Genes (Homo sapiens)
CDC42  (cell division cycle 42)
RAB27A  (RAB27A, member RAS oncogene family)
RAB3A  (RAB3A, member RAS oncogene family)
STX1A  (syntaxin 1A)
STXBP1  (syntaxin binding protein 1)
UNC13A  (unc-13 homolog A)
VAMP2  (vesicle associated membrane protein 2)


Additional Information