A conserved regulatory mode in exocytic membrane fusion revealed by Mso1p membrane interactions

Weber-Boyvat, Marion; Zhao, Hongxia; Aro, Nina; Yuan, Qiang; Chernov, Konstantin G.; Peränen, Johan; Lappalainen, Pekka; Jäntti, Jussi

doi:10.1091/mbc.e12-05-0415

Cited by 6 publications

(4 citation statements)

References 41 publications

(41 reference statements)

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“…This is potentially consistent with Sec1 functioning at the end of vesicle tethering, rapidly disappearing around the moment of membrane fusion. Mso1, a small nonessential protein tightly associated with Sec1 and suggested to be an effector of Sec4, was found to have a similarly short lifetime, not significantly different from Sec1 (median 2.5 s, mean 2.6 s; Figure 5A ; Weber et al, 2010 ; Weber-Boyvat et al, 2013 ).…”

Section: Resultsmentioning

confidence: 97%

High-resolution secretory timeline from vesicle formation at the Golgi to fusion at the plasma membrane in S. cerevisiae

Gingras

Sulpizio

Park

et al. 2022

eLife

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Most of the components in the yeast secretory pathway have been studied, yet a high-resolution temporal timeline of their participation is lacking. Here we define the order of acquisition, lifetime, and release of critical components involved in late secretion from the Golgi to the plasma membrane. Of particular interest is the timing of the many reported effectors of the secretory vesicle Rab protein Sec4, including the myosin-V Myo2, the exocyst complex, the lgl homolog Sro7, and the small yeast-specific protein Mso1. At the trans-Golgi network (TGN) Sec4's GEF, Sec2, is recruited to Ypt31-positive compartments, quickly followed by Sec4 and Myo2 and vesicle formation. While transported to the bud tip, the entire exocyst complex, including Sec3, is assembled on to the vesicle. Before fusion, vesicles tether for 5s, during which the vesicle retains the exocyst complex and stimulates lateral recruitment of Rho3 on the plasma membrane. Sec2 and Myo2 are rapidly lost, followed by recruitment of cytosolic Sro7, and finally the SM protein Sec1, which appears for just 2 seconds prior to fusion. Perturbation experiments reveal an ordered and robust series of events during tethering that provide insights into the function of Sec4 and effector exchange.

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Section: Resultsmentioning

confidence: 97%

High-resolution secretory timeline from vesicle formation at the Golgi to fusion at the plasma membrane in S. cerevisiae

Gingras

Sulpizio

Park

et al. 2022

eLife

View full text Add to dashboard Cite

show abstract

“…This is potentially consistent with Sec1 functioning at the end of vesicle tethering, rapidly disappearing around the moment of membrane fusion. Mso1, a small nonessential protein tightly associated with Sec1 and suggested to be an effector of Sec4, was found to have a similarly short lifetime, not significantly different from Sec1 (median 2.5s, mean 2.6s; Figure 5A)(Weber et al, 2010; Weber-Boyvat et al, 2012).…”

Section: Resultsmentioning

confidence: 99%

High-resolution secretory timeline from vesicle formation at the Golgi to fusion at the plasma membrane in S. cerevisiae

Gingras

Sulpizio

Park

et al. 2022

Preprint

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Most of the components in the yeast secretory pathway have been studied, yet a high resolution temporal timeline of their participation is lacking. Here we define the order of acquisition, lifetime, and release of critical components involved in late secretion from the Golgi to the plasma membrane. Of particular interest is the timing of the many reported effectors of the secretory vesicle Rab protein Sec4, including the myosin-V Myo2, the exocyst complex, the lgl homolog Sro7, and the small yeast-specific protein Mso1. At the trans-Golgi network (TGN) Sec4's GEF, Sec2, is recruited to Ypt31-positive compartments, quickly followed by Sec4 and Myo2 and vesicle formation. While transported to the bud tip, the entire exocyst complex, including Sec3, is assembled on to the vesicle. Before fusion, vesicles tether for 5s, during which the vesicle retains the exocyst complex and stimulates lateral recruitment of Rho3 on the plasma membrane. Sec2 and Myo2 are rapidly lost, followed by recruitment of cytosolic Sro7, and finally the SM protein Sec1, which appears for just 2 seconds prior to fusion. Perturbation experiments reveal an ordered and robust series of events during tethering that provide insights into the function of Sec4 and effector exchange.

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“…, 1997 ). Mso1 has also been shown to interact with the membrane and is suggested to interact with both the target membrane and the vesicle membrane ( Weber-Boyvat et al. , 2013 ).…”

Section: Introductionmentioning

confidence: 99%

Roles of Mso1 and the SM protein Sec1 in efficient vesicle fusion during fission yeast cytokinesis

Gerien

Zhang

Russell

et al. 2020

MBoC

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A conserved regulatory mode in exocytic membrane fusion revealed by Mso1p membrane interactions

Cited by 6 publications

References 41 publications

High-resolution secretory timeline from vesicle formation at the Golgi to fusion at the plasma membrane in S. cerevisiae

High-resolution secretory timeline from vesicle formation at the Golgi to fusion at the plasma membrane in S. cerevisiae

High-resolution secretory timeline from vesicle formation at the Golgi to fusion at the plasma membrane in S. cerevisiae

Roles of Mso1 and the SM protein Sec1 in efficient vesicle fusion during fission yeast cytokinesis

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