The t-SNAREs syntaxin4 and SNAP23 but not v-SNARE VAMP2 are indispensable to tether GLUT4 vesicles at the plasma membrane in adipocyte

Kawaguchi, Takayuki; Tamori, Yoshikazu; Kanda, Hajime; Yoshikawa, Mitsuo; Tateya, Sanshiro; Nishino, Naonobu; Kasuga, Masato

doi:10.1016/j.bbrc.2009.12.045

Cited by 29 publications

(35 citation statements)

References 27 publications

(29 reference statements)

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“…we have reported that introduction of the cytosolic domain of VAMP2 (but not VAMP3 or VAMP4) inhibits GLUT4 translocation in permeabilized 3T3‐L1 adipocytes (19). Consistent with this, a recent study from Kasuga's group also reported a significant inhibition of insulin‐stimulated glucose transport and GLUT4 translocation in 3T3‐L1 adipocytes depleted of VAMP2 using siRNA (17).…”

Section: Snare Proteins At the Plasma Membranesupporting

confidence: 79%

“…For example, homozygotic disruption of the Sx4 gene results in early embryonic lethality, but heterozygote (Sx4 +/−) knockout mice exhibit impaired glucose tolerance, with a 50% reduction in whole‐body glucose uptake, a result attributed to an approximate 50% reduction in insulin‐stimulated glucose uptake and GLUT4 translocation in skeletal muscle (16). Similarly, depletion of Sx4 or S‐23 using siRNA revealed that these plasma membrane SNAREs are essential for GLUT4–vesicle fusion with the plasma membrane (17).…”

Section: Snare Proteins At the Plasma Membranementioning

confidence: 99%

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SNARE Proteins Underpin Insulin‐Regulated GLUT4 Traffic

Bryant

Gould

2011

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Delivery of the glucose transporter type 4 (GLUT4) from an intracellular location to the cell surface in response to insulin represents a specialized form of membrane traffic, known to be impaired in the disease states of insulin resistance and type 2 diabetes. Like all membrane trafficking events, this translocation of GLUT4 requires members of the SNARE family of proteins. Here, we discuss two SNARE complexes that have been implicated in insulin-regulated GLUT4 traffic: one regulating the final delivery of GLUT4 to the cell surface in response to insulin and the other controlling GLUT4's intracellular trafficking.

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Section: Snare Proteins At the Plasma Membranesupporting

confidence: 79%

Section: Snare Proteins At the Plasma Membranementioning

confidence: 99%

SNARE Proteins Underpin Insulin‐Regulated GLUT4 Traffic

Bryant

Gould

2011

Traffic

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“…A body of work examining elements of this step concluded earlier on that VAMP2 on the GLUT4 vesicle and syntaxin4 and SNAP23 on the plasma membrane are required for GLUT4 vesicle fusion in muscle and adipose cells (19,30,40). A body of work examining elements of this step concluded earlier on that VAMP2 on the GLUT4 vesicle and syntaxin4 and SNAP23 on the plasma membrane are required for GLUT4 vesicle fusion in muscle and adipose cells (19,30,40).…”

Section: Vamp2 Syntaxin4 and Snap23: The "Fusion Machinery" For Glumentioning

confidence: 99%

Signal transduction meets vesicle traffic: the software and hardware of GLUT4 translocation

Klip

Sun

Chiu

et al. 2014

American Journal of Physiology-Cell Physiology

136

105

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Skeletal muscle is the major tissue disposing of dietary glucose, a function regulated by insulin-elicited signals that impart mobilization of GLUT4 glucose transporters to the plasma membrane. This phenomenon, also central to adipocyte biology, has been the subject of intense and productive research for decades. We focus on muscle cell studies scrutinizing insulin signals and vesicle traffic in a spatiotemporal manner. Using the analogy of an integrated circuit to approach the intersection between signal transduction and vesicle mobilization, we identify signaling relays ("software") that engage structural/mechanical elements ("hardware") to enact the rapid mobilization and incorporation of GLUT4 into the cell surface. We emphasize how insulin signal transduction switches from tyrosine through lipid and serine phosphorylation down to activation of small G proteins of the Rab and Rho families, describe key negative regulation step of Rab GTPases through the GTPase-activating protein activity of the Akt substrate of 160 kDa (AS160), and focus on the mechanical effectors engaged by Rabs 8A and 10 (the molecular motor myosin Va), and the Rho GTPase Rac1 (actin filament branching and severing through Arp2/3 and cofilin). Finally, we illustrate how actin filaments interact with myosin 1c and α-Actinin4 to promote vesicle tethering as preamble to fusion with the membrane.

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“…Disrupting the function of these molecules (e.g. using antibody microinjection, transgenic knockout or siRNA approaches) supports a role for these proteins in the insulin-stimulated delivery of GLUT4 to the cell surface (see, for example, [9,[11][12][13]). Consistent with this, Sx4/SNAP23-containing liposomes could fuse with liposomes containing VAMP2, providing functional evidence that this SNARE combination is sufficient to drive membrane fusion in vitro [14].…”

mentioning

confidence: 98%

“…Subsequent studies have indicated the VAMP2 (vesicleassociated membrane protein 2) isoform as being the key v-SNARE in GSVs (reviewed in [9], but, for an alternative view, see [10]). Studies from numerous laboratories identified Sx4 (syntaxin 4) and SNAP23 (23 kDa synaptosome-associated protein) as the key t-SNAREs on the plasma membrane of adipocytes [9,11]. Disrupting the function of these molecules (e.g.…”

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confidence: 99%

Studies of the regulated assembly of SNARE complexes in adipocytes

Kioumourtzoglou

Sadler

Black

et al. 2014

Biochemical Society Transactions

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Insulin plays a fundamental role in whole-body glucose homeostasis. Central to this is the hormone's ability to rapidly stimulate the rate of glucose transport into adipocytes and muscle cells [1]. Upon binding its receptor, insulin stimulates an intracellular signalling cascade that culminates in redistribution of glucose transporter proteins, specifically the GLUT4 isoform, from intracellular stores to the plasma membrane, a process termed 'translocation' [1,2]. This is an example of regulated membrane trafficking [3], a process that also underpins other aspects of physiology in a number of specialized cell types, for example neurotransmission in brain/neurons and release of hormone-containing vesicles from specialized secretory cells such as those found in pancreatic islets. These processes invoke a number of intriguing biological questions as follows. How is the machinery involved in these membrane trafficking events mobilized in response to a stimulus? How do the signalling pathways that detect the external stimulus interface with the trafficking machinery? Recent studies of insulin-stimulated GLUT4 translocation offer insight into such questions. In the present paper, we have reviewed these studies and draw parallels with other regulated trafficking systems.

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The t-SNAREs syntaxin4 and SNAP23 but not v-SNARE VAMP2 are indispensable to tether GLUT4 vesicles at the plasma membrane in adipocyte

Cited by 29 publications

References 27 publications

SNARE Proteins Underpin Insulin‐Regulated GLUT4 Traffic

SNARE Proteins Underpin Insulin‐Regulated GLUT4 Traffic

Signal transduction meets vesicle traffic: the software and hardware of GLUT4 translocation

Studies of the regulated assembly of SNARE complexes in adipocytes

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