Syntaxin 6 functions in trans-Golgi network vesicle trafficking.

Bock, Jason B.; Klumperman, Judith; Davanger, Svend; Scheller, Richard H.

doi:10.1091/mbc.8.7.1261

Cited by 282 publications

(259 citation statements)

References 46 publications

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“…The Golgi apparatus is involved in vesicular traffic. A number of SNARE proteins, such as yeast Sed5p (Banfield et al, 1994) and mVps45 (Tellam et al, 1997), mammalian syntaxin 6 (Bock et al, 1997), VAMP4, Syntaxin 13, and mVtib (Advani et al, 1998), have all been reported to be localized to the Golgi. Rat munc13-1 has been shown to interact with a number of proteins involved in vesicle docking and trafficking, such as syntaxin (Betz et al, 1997) and Doc2 (Orita et al, 1997).…”

Section: Discussionmentioning

confidence: 99%

Human munc13 Is a Diacylglycerol Receptor that Induces Apoptosis and May Contribute to Renal Cell Injury in Hyperglycemia

Song

Ailenberg

Silverman

1999

MBoC

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We have previously shown that human munc13 (hmunc13) is up-regulated by hyperglycemia under in vitro conditions in human mesangial cell cultures. The purpose of the present study was to determine the cellular function of hmunc13. To do this, we have investigated the subcellular localization of hmunc13 in a transiently transfected renal cell line, opossum kidney cells. We have found that hmunc13 is a cytoplasmic protein and is translocated to the Golgi apparatus after phorbol ester stimulation. In addition, cells transfected with hmunc13 demonstrate apoptosis after treatment with phorbol ester, but cells transfected with an hmunc13 deletion mutant in which the diacylglycerol (C1) binding domain is absent exhibit no change in intracellular distribution and no induction of apoptosis in the presence of phorbol ester stimulation. We conclude that both the diacylglycerol-induced translocation and the apoptosis represent functional activity of hmunc13. We have also demonstrated that munc13-1 and munc13-2 are localized mainly to cortical epithelial cells in rat kidney and both are overexpressed under conditions of hyperglycemia in a streptozotocin-treated diabetic rat model. Taken together, our data suggest that hmunc13 serves as a diacylglycerol-activated, PKC-independent signaling pathway capable of inducing apoptosis and that this pathway may contribute to the renal cell complications of hyperglycemia.

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Section: Discussionmentioning

confidence: 99%

Human munc13 Is a Diacylglycerol Receptor that Induces Apoptosis and May Contribute to Renal Cell Injury in Hyperglycemia

Song

Ailenberg

Silverman

1999

MBoC

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“…Syntaxin 6 is a trans-Golgi network protein and regulates membrane trafficking (36). Partial colocalization of CDCP1-containing vesicles with syntaxin Fig.…”

Section: Cdcp1 Localizes To Lipid Raft-containing Vesicular Structurementioning

confidence: 99%

CDCP1 Regulates the Function of MT1-MMP and Invadopodia-Mediated Invasion of Cancer Cells

Miyazawa

Uekita

Ito

et al. 2013

Molecular Cancer Research

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Complement C1r/C1s, Uegf, Bmp1 (CUB) domain-containing protein 1 (CDCP1) is a transmembrane protein that regulates anchorage-independent growth and cancer cell migration and invasion. Expression of CDCP1 is detected in a number of cancer cell lines and tissues and is closely correlated with poor prognosis. Invadopodia are actin-based protrusions on the surface of invasive cancer cells that promote the degradation of the extracellular matrix (ECM) via localized proteolysis, which is mainly mediated by membrane type 1 matrix metalloproteinase (MT1-MMP). MT1-MMP is accumulated at invadopodia by targeted delivery via membrane trafficking. The present study shows that CDCP1 is required for ECM degradation by invadopodia in human breast cancer and melanoma cells. CDCP1 localized to caveolin-1-containing vesicular structures and lipid rafts and was detected in close proximity to invadopodia. Further biochemical analysis revealed that substantial amounts of CDCP1 existed in the Triton X-100 insoluble lipid raft fraction. CDCP1 was coimmunoprecipitated with MT1-MMP and colocalized with MT1-MMP at the vesicular structures. The siRNA-mediated knockdown of the CDCP1 expression markedly inhibited MT1-MMP-dependent ECM degradation and Matrigel invasion and reduced the accumulation of MT1-MMP at invadopodia, as shown by immunofluorescence analysis. These results indicate that CDCP1 is an essential regulator of the trafficking and function of MT1-MMP-and invadopodia-mediated invasion of cancer cells. Mol Cancer Res; 11(6); 628-37.

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“…Rabbit antisera for sec22b (Hay et al, 1998), VAMP2 (Pevsner et al, 1994), and VAMP4 (Steegmaier et al, 1999), and mouse mAbs for rbet1 (Hay et al, 1998), syntaxin 1 (Inoue et al, 1992), syntaxin 6 (Bock et al, 1997), and syntaxin 13 (Prekeris et al, 1998), have been described previously. Antibodies for calnexin, cytochrome C, human LAMP1, and myc (clone 9E10) were purchased from Stressgen (Victoria, British Columbia, Canada), PharMingen (San Diego, CA), Transduction Laboratories (Lexington, KY), and Santa Cruz Biotechnology (Santa Cruz, CA), respectively.…”

Section: Antibodiesmentioning

confidence: 99%

Syntaxin 17 Is Abundant in Steroidogenic Cells and Implicated in Smooth Endoplasmic Reticulum Membrane Dynamics

Steegmaier

Oorschot

Klumperman

et al. 2000

MBoC

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The endoplasmic reticulum (ER) consists of subcompartments that have distinct protein constituents, morphological appearances, and functions. To understand the mechanisms that regulate the intricate and dynamic organization of the endoplasmic reticulum, it is important to identify and characterize the molecular machinery involved in the assembly and maintenance of the different subcompartments. Here we report that syntaxin 17 is abundantly expressed in steroidogenic cell types and specifically localizes to smooth membranes of the ER. By immunoprecipitation analyses, syntaxin 17 exists in complexes with a syntaxin regulatory protein, rsly1, and/or two intermediate compartment SNARE proteins, rsec22b and rbet1. Furthermore, we found that syntaxin 17 is anchored to the smooth endoplasmic reticulum through an unusual mechanism, requiring two adjacent hydrophobic domains near its carboxyl terminus. Converging lines of evidence indicate that syntaxin 17 functions in a vesicle-trafficking step to the smooth-surfaced tubular ER membranes that are abundant in steroidogenic cells.

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Syntaxin 6 functions in trans-Golgi network vesicle trafficking.

Cited by 282 publications

References 46 publications

Human munc13 Is a Diacylglycerol Receptor that Induces Apoptosis and May Contribute to Renal Cell Injury in Hyperglycemia

Human munc13 Is a Diacylglycerol Receptor that Induces Apoptosis and May Contribute to Renal Cell Injury in Hyperglycemia

CDCP1 Regulates the Function of MT1-MMP and Invadopodia-Mediated Invasion of Cancer Cells

Syntaxin 17 Is Abundant in Steroidogenic Cells and Implicated in Smooth Endoplasmic Reticulum Membrane Dynamics

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