The Sec15 protein responds to the function of the GTP binding protein, Sec4, to control vesicular traffic in yeast.

Salminen, Antti; Novick, Peter

doi:10.1083/jcb.109.3.1023

Cited by 134 publications

(120 citation statements)

References 30 publications

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“…We observed no suppression of the temperature sensitivity of sec15-1 by a high copy number BEM1 plasmid (data not shown). Upon PCR-based genomic sequencing of the sec15-1 allele, we determined that a point mutation of a single base pair (G to T) at position 2506 resulted in premature termination of the protein and loss of the last 76 amino acids at the Cterminus, which is consistent with the observation that the mutant protein is shifted to a higher mobility by SDS-PAGE analysis (Salminen and Novick, 1989).…”

Section: Resultssupporting

confidence: 78%

“…One effector of Sec4p is the exocyst -an octameric complex composed of Sec3p, Sec5p, Sec6p, Sec8p, Sec10p, Sec15p, Exo70p and Exo84p -that has been implicated in tethering secretory vesicles to the plasma membrane. Sec15p has been shown to interact genetically as well as physically with activated Sec4p, making it a documented effector of Sec4p (Guo et al, 1999b;Salminen and Novick, 1989). All components of the exocyst complex localize to sites of active exocytosis (Guo et al, 1999a;Guo et al, 1999b;TerBush et al, 1996).…”

Section: Introductionmentioning

confidence: 99%

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The polarity-establishment component Bem1p interacts with the exocyst complex through the Sec15p subunit

Boyd

Coleman

Novick

2006

Journal of Cell Science

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Section: Resultssupporting

confidence: 78%

Section: Introductionmentioning

confidence: 99%

The polarity-establishment component Bem1p interacts with the exocyst complex through the Sec15p subunit

Boyd

Coleman

Novick

2006

Journal of Cell Science

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“…In the yeast secretory pathway, overexpression of the exocyst subunit Sec15, an effector protein of Sec4, leads to the formation of a cluster of secretory vesicles and a patch of Sec15 close to the plasma membrane that colocalizes with Sec4 (Salminen and Novick, 1989). The ability of Sec15 to form this patch depends on Sec4 and Sec2, a GEF for Sec4 (Salminen and Novick, 1989).…”

Section: Discussionmentioning

confidence: 99%

The CORVET Subunit Vps8 Cooperates with the Rab5 Homolog Vps21 to Induce Clustering of Late Endosomal Compartments

Markgraf

Ahnert

Arlt

et al. 2009

MBoC

124

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Membrane tethering, the process of mediating the first contact between membranes destined for fusion, requires specialized multisubunit protein complexes and Rab GTPases. In the yeast endolysosomal system, the hexameric HOPS tethering complex cooperates with the Rab7 homolog Ypt7 to promote homotypic fusion at the vacuole, whereas the recently identified homologous CORVET complex acts at the level of late endosomes. Here, we have further functionally characterized the CORVET-specific subunit Vps8 and its relationship to the remaining subunits using an in vivo approach that allows the monitoring of late endosome biogenesis. In particular, our results indicate that Vps8 interacts and cooperates with the activated Rab5 homolog Vps21 to induce the clustering of late endosomal membranes, indicating that Vps8 is the effector subunit of the CORVET complex. This clustering, however, requires Vps3, Vps16, and Vps33 but not the remaining CORVET subunits. These data thus suggest that the CORVET complex is built of subunits with distinct activities and potentially, their sequential assembly could regulate tethering and successive fusion at the late endosomes.

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“…Interestingly, overexpression of these proteins also leads to clustering of Sec4-containing secretory vesicles (Rossi and Brennwald, 2011;Salminen and Novick, 1989). Since Bem3 and Sec4 colocalized extensively, we tested whether the intracellular localization of Bem3 could be also influenced by Sec15 or Sro7.…”

Section: S29nmentioning

confidence: 99%

Bem3, a Cdc42 GTPase-Activating Protein, traffics to an intracellular compartment and recruits the secretory Rab GTPase Sec4 to endomembranes

Mukherjee

Sen

Boettner

et al. 2013

Journal of Cell Science

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SummaryCell polarity is essential for many cellular functions including division and cell-fate determination. Although RhoGTPase signaling and vesicle trafficking are both required for the establishment of cell polarity, the mechanisms by which they are coordinated are unclear. Here, we demonstrate that the yeast RhoGAP (GTPase activating protein), Bem3, is targeted to sites of polarized growth by the endocytic and recycling pathways. Specifically, deletion of SLA2 or RCY1 led to mislocalization of Bem3 to depolarized puncta and accumulation in intracellular compartments, respectively. Bem3 partitioned between the plasma membrane and an intracellular membrane-bound compartment. These Bem3-positive structures were polarized towards sites of bud emergence and were mostly observed during the pre-mitotic phase of apical growth. Cell biological and biochemical approaches demonstrated that this intracellular Bem3 compartment contained markers for both the endocytic and secretory pathways, which were reminiscent of the Spitzenkörper present in the hyphal tips of growing fungi. Importantly, Bem3 was not a passive cargo, but recruited the secretory Rab protein, Sec4, to the Bem3-containing compartments. Moreover, Bem3 deletion resulted in less efficient localization of Sec4 to bud tips during early stages of bud emergence. Surprisingly, these effects of Bem3 on Sec4 were independent of its GAP activity, but depended on its ability to efficiently bind endomembranes. This work unveils unsuspected and important details of the relationship between vesicle traffic and elements of the cell polarity machinery: (1) Bem3, a cell polarity and peripherally associated membrane protein, relies on vesicle trafficking to maintain its proper localization; and (2) in turn, Bem3 influences secretory vesicle trafficking.

show abstract

The Sec15 protein responds to the function of the GTP binding protein, Sec4, to control vesicular traffic in yeast.

Cited by 134 publications

References 30 publications

The polarity-establishment component Bem1p interacts with the exocyst complex through the Sec15p subunit

The polarity-establishment component Bem1p interacts with the exocyst complex through the Sec15p subunit

The CORVET Subunit Vps8 Cooperates with the Rab5 Homolog Vps21 to Induce Clustering of Late Endosomal Compartments

Bem3, a Cdc42 GTPase-Activating Protein, traffics to an intracellular compartment and recruits the secretory Rab GTPase Sec4 to endomembranes

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