Syntaxin 4 in 3T3-L1 adipocytes: regulation by insulin and participation in insulin-dependent glucose transport.

Volchuk, Allen; Wang, Q; Ewart, H. Stephen; Liu, Z; He, Lijing; Bennett, Mark K.; Klip, Amira

doi:10.1091/mbc.7.7.1075

Cited by 136 publications

(122 citation statements)

References 38 publications

Supporting

Mentioning

111

Contrasting

Order By: Relevance

“…The fidelity of this process is mediated at least in part by SNARE proteins [27]. In adipocytes and muscle, the SNAREs syntaxin 4 and VAMP2 have been identified as being of crucial importance in insulin-stimulated GLUT4 translocation [7,12,28,29]. We have previously demonstrated that expression of syntaxin 4 and VAMP2 is increased in muscles derived from SHRSP animals compared with in WKY animals [6], in addition to in the Zucker diabetic fatty rat [30].…”

Section: Discussionmentioning

confidence: 98%

Reduced insulin-stimulated GLUT4 bioavailability in stroke-prone spontaneously hypertensive rats

et al. 2005

View full text Add to dashboard Cite

Aims/hypothesis: Insulin-stimulated glucose transport is impaired in a genetic model of hypertension, the stroke-prone spontaneously hypertensive rat (SHRSP), yet the molecular mechanisms that underlie this defect in the animals remain unclear. Methods: We examined the effects of insulin on the trafficking of the insulin-responsive glucose transporter GLUT4 to the plasma membrane in isolated adipocytes from SHRSP and normotensive control WistarKyoto (WKY) rats. Results: Treatment of isolated adipocytes with insulin resulted in trafficking of GLUT4 to the plasma membrane. There was no significant difference in the magnitude of insulin-stimulated GLUT4 trafficking from intracellular membranes to the plasma membrane between strains. In contrast, we demonstrated that there is a significant reduction in GLUT4 accessible to the glucose photolabel Bio-LC-ATB-BGPA at the plasma membrane of SHRSP adipocytes compared with control rats. Conclusions/ interpretation: We propose that a large proportion of GLUT4 translocated to the plasma membrane in response to insulin is not able to bind substrate and catalyse transport in the SHRSP. Therefore, there is a reduction in bioavailable GLUT4 in SHRSP animals that is likely to account, at least in part, for the reduced insulin-stimulated glucose uptake.

show abstract

Section: Discussionmentioning

confidence: 98%

Reduced insulin-stimulated GLUT4 bioavailability in stroke-prone spontaneously hypertensive rats

et al. 2005

View full text Add to dashboard Cite

show abstract

“…In contrast, the presence of syntaxins 3 and 4 on either the apical or basolateral surface, respectively, strongly suggests that they are involved in polarized vesicular transport pathways to these surfaces. It is interesting that syntaxin 3 is not expressed in adipocytes (Volchuk et al, 1996), which do not possess an apical surface, or in hepatocytes (Figure 1; Bennett et al, 1993), which have an apical plasma membrane but lack a direct pathway from the TGN to this surface (Hubbard, 1991). Together, this might suggest that syntaxin 3 functions at the apical surface of polarized cells and could be potentially involved in the biosynthetic pathway.…”

Section: Discussionmentioning

confidence: 99%

“…Similarly, this work has generally examined the role of a single v-SNARE/t-SNARE combination. To our knowledge, only two reports have examined the role of multiple syntaxin isoforms in a single, nonpolarized cell type, i.e., in adipocytes (Volchuk et al, 1996) and macrophages (Hackam et al, 1996).…”

Section: Introductionmentioning

confidence: 99%

Differential localization of syntaxin isoforms in polarized Madin-Darby canine kidney cells.

Low

Chapin

Weimbs

et al. 1996

MBoC

Self Cite

225

223

View full text Add to dashboard Cite

Syntaxins, integral membrane proteins that are part of the ubiquitous membrane fusion machinery, are thought to act as target membrane receptors during the process of vesicle docking and fusion. Several isoforms of the syntaxin family have been previously identified in mammalian cells, some of which are localized to the plasma membrane. We investigated the subcellular localization of these putative plasma membrane syntaxins in polarized epithelial cells, which are characterized by the presence of distinct apical and basolateral plasma membrane domains. Syntaxins 2, 3, and 4 were found to be endogenously present in Madin-Darby canine kidney cells. The localization of syntaxins 1A, 1B, 2, 3, and 4 in stably transfected Madin-Darby canine kidney cell lines was studied with confocal immunofluorescence microscopy. Each syntaxin isoform was found to have a unique pattern of localization. Syntaxins 1A and 1B were present only in intracellular structures, with little or no apparent plasma membrane staining. In contrast, syntaxin 2 was found on both the apical and basolateral surface, whereas the plasma membrane localization of syntaxins 3 and 4 were restricted to the apical or basolateral domains, respectively. Syntaxins are therefore the first known components of the plasma membrane fusion machinery that are differentially localized in polarized cells, suggesting that they may play a central role in targeting specificity.

show abstract

“…Specific SNARE isoforms are expressed in muscle and fat cells, i.e., VAMP2 and VAMP3/cellubrevin (hereafter called VAMP3) (Cain et al, 1992;Volchuk et al, 1994Volchuk et al, , 1995, syntaxin4 Volchuk et al, 1996), and SNAP-23 (SNAP-25-like protein of 23 kDa) (Wang et al, 1997;Wong et al, 1997;Rea et al, 1998). The participation of the target membrane (t)-SNAREs syntaxin4 (Cheatham et al, 1996;Olson et al, 1997) and SNAP-23 (Rea et al, 1998;Foran et al, 1999;Foster et al, 1999b) in GLUT4 translocation has been implicated with the use of various molecular and biochemical approaches, such as the introduction of botulinum toxins and neutralizing antibodies into 3T3-L1 adipocytes.…”

Section: Introductionmentioning

confidence: 99%

VAMP2, but Not VAMP3/Cellubrevin, Mediates Insulin-dependent Incorporation of GLUT4 into the Plasma Membrane of L6 Myoblasts

Randhawa

Bilan

Khayat

et al. 2000

MBoC

102

117

View full text Add to dashboard Cite

Like neuronal synaptic vesicles, intracellular GLUT4-containing vesicles must dock and fuse with the plasma membrane, thereby facilitating insulin-regulated glucose uptake into muscle and fat cells. GLUT4 colocalizes in part with the vesicle SNAREs VAMP2 and VAMP3. In this study, we used a single-cell fluorescence-based assay to compare the functional involvement of VAMP2 and VAMP3 in GLUT4 translocation. Transient transfection of proteolytically active tetanus toxin light chain cleaved both VAMP2 and VAMP3 proteins in L6 myoblasts stably expressing exofacially myc-tagged GLUT4 protein and inhibited insulin-stimulated GLUT4 translocation. Tetanus toxin also caused accumulation of the remaining C-terminal VAMP2 and VAMP3 portions in Golgi elements. This behavior was exclusive to these proteins, because the localization of intracellular myc-tagged GLUT4 protein was not affected by the toxin. Upon cotransfection of tetanus toxin with individual vesicle SNARE constructs, only toxin-resistant VAMP2 rescued the inhibition of insulin-dependent GLUT4 translocation by tetanus toxin. Moreover, insulin caused a cortical actin filament reorganization in which GLUT4 and VAMP2, but not VAMP3, were clustered. We propose that VAMP2 is a resident protein of the insulin-sensitive GLUT4 compartment and that the integrity of this protein is required for GLUT4 vesicle incorporation into the cell surface in response to insulin.

show abstract

Syntaxin 4 in 3T3-L1 adipocytes: regulation by insulin and participation in insulin-dependent glucose transport.

Cited by 136 publications

References 38 publications

Reduced insulin-stimulated GLUT4 bioavailability in stroke-prone spontaneously hypertensive rats

Reduced insulin-stimulated GLUT4 bioavailability in stroke-prone spontaneously hypertensive rats

Differential localization of syntaxin isoforms in polarized Madin-Darby canine kidney cells.

VAMP2, but Not VAMP3/Cellubrevin, Mediates Insulin-dependent Incorporation of GLUT4 into the Plasma Membrane of L6 Myoblasts

Contact Info

Product

Resources

About