Multiple Pathways Regulate Endocytic Coat Disassembly in<i> Saccharomyces cerevisiae</i> for Optimal Downstream Trafficking

Toret, Christopher P.; Lee, Linda; Sekiya-Kawasaki, Mariko; Drubin, David G.

doi:10.1111/j.1600-0854.2008.00726.x

Cited by 63 publications

(71 citation statements)

References 32 publications

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“…Studies using C-terminally tagged epsins and AP180s have given slightly varying dynamics in some cases than we observed using N-terminal tags (Carroll et al, 2012;Toret et al, 2008). It is possible that N-terminal fusions affect the membrane binding ENTH/ANTH domains.…”

Section: Resultsmentioning

confidence: 66%

“…A similar phenotype is observed when the Pan1 sites phosphorylated by Prk1 are mutated to Ala (Toshima et al, 2005). Since recruitment of Prk1 and Ark1 during endocytosis is late during the actin phase (Toret et al, 2008;Zeng et al, 2007), these kinases are thought to negatively regulate endocytic factors and/or promote uncoating of endocytic vesicles after scission.…”

Section: Introductionmentioning

confidence: 66%

“…Prk1 substrates are hyper-phosphorylated in cells mutant for the Scd5 PP1 binding site Phosphorylation of several immobile phase endocytic factors by Prk1 (and Ark1) promotes coat disassembly at the end of internalization (Chang et al, 2006;Cope et al, 1999;Toret et al, 2008;Toshima et al, 2005;Watson et al, 2001;Zeng et al, 2001). If Scd5 targets PP1/Glc7 to these factors, mutation of the Scd5 PP1 binding site should result in their hyperphosphorylation.…”

Section: Resultsmentioning

confidence: 99%

“…Prk1, the best studied of these kinases, has been shown to phosphorylate a number of downstream targets in the yeast proteome, but the predominant targets are cortical actin patch/endocytic factors, particularly coat module factors that arrive during the immobile phase of internalization (Breitkreutz et al, 2010;Henry et al, 2003;Huang et al, 2003;Mok et al, 2010;Ptacek et al, 2005;Toret et al, 2008;Toshima et al, 2005;Watson et al, 2001;Zeng and Cai, 1999;Zeng et al, 2001). Here we showed that several of these endocytic Prk1 substrates, Pan1, Sla1, Ent1/2, and Yap1801/ 2, are hyperphosphorylated in scd5-PP1D2 cells, thus each of these proteins are likely targets of Scd5/PP1.…”

Section: Hyperphosphorylation Perturbs Endocytic Vesicle Formation Anmentioning

confidence: 99%

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Role of Scd5, a protein phosphatase-1 targeting protein, in phosphoregulation of Sla1 during endocytosis

Richard¹,

Torres²,

Segarra³

et al. 2012

Journal of Cell Science

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SummaryPhosphorylation regulates assembly and disassembly of proteins during endocytosis. In yeast, Prk1 and Ark1 phosphorylate factors after vesicle internalization leading to coat disassembly. Scd5, a protein phosphatase-1 (PP1)-targeting subunit, is proposed to regulate dephosphorylation of Prk1/Ark1 substrates to promote new rounds of endocytosis. In this study we analyzed scd5-PP1D2, a mutation causing impaired PP1 binding. scd5-PP1D2 caused hyperphosphorylation of several Prk1 endocytic targets. Live-cell imaging of 15 endocytic components in scd5-PP1D2 revealed that most factors arriving before the invagination/actin phase of endocytosis had delayed lifetimes. Severely affected were early factors and Sla2 (Hip1R homolog), whose lifetime was extended nearly fourfold. In contrast, the lifetime of Sla1, a Prk1 target, was extended less than twofold, but its cortical recruitment was significantly reduced. Delayed Sla2 dynamics caused by scd5-PP1D2 were suppressed by SLA1 overexpression. This was dependent on the LxxQxTG repeats (SR) of Sla1, which are phosphorylated by Prk1 and bind Pan1, another Prk1 target, in the dephosphorylated state. Without the SR, Sla1DSR was still recruited to the cell surface, but was less concentrated in cortical patches than Pan1. sla1DSR severely impaired endocytic progression, but this was partially suppressed by overexpression of LAS17, suggesting that without the SR region the SH3 region of Sla1 causes constitutive negative regulation of Las17 (WASp). These results demonstrate that Scd5/PP1 is important for recycling Prk1 targets to initiate new rounds of endocytosis and provide new mechanistic information on the role of the Sla1 SR domain in regulating progression to the invagination/actin phase of endocytosis.

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Section: Resultsmentioning

confidence: 66%

Section: Introductionmentioning

confidence: 66%

Section: Resultsmentioning

confidence: 99%

Section: Hyperphosphorylation Perturbs Endocytic Vesicle Formation Anmentioning

confidence: 99%

See 2 more Smart Citations

Role of Scd5, a protein phosphatase-1 targeting protein, in phosphoregulation of Sla1 during endocytosis

Richard¹,

Torres²,

Segarra³

et al. 2012

Journal of Cell Science

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“…Several studies suggested that with respect to the timing of membrane recruitment (Toret et al, 2008) and interactions with the endocytic machinery (Rosenthal et al, 1999;Aguilar et al, 2003) epsin paralogs behave similarly. No data are available, however, regarding potential signaling redundancy among epsin family members.…”

Section: Introductionmentioning

confidence: 99%

The yeast endocytic protein Epsin 2 functions in a cell-division signaling pathway

Mukherjee

Coon

Edwards

et al. 2009

Journal of Cell Science

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The epsins are a family of adaptors involved in recruiting other endocytic proteins, binding of ubiquitylated cargo and induction of membrane curvature. These molecules bear a characteristic epsin N-terminal homology (ENTH) domain and multiple peptide motifs that mediate protein-protein interactions. We have previously demonstrated that the ENTH domain of epsin is involved in Cdc42 signaling regulation. Here, we present evidence that yeast epsin 2 (Ent2) plays a signaling role during cell division. We observed that overexpression of the ENTH domain of Ent2 (ENTH2), but not Ent1, promoted the formation of chains of cells and aberrant septa. This dominant-negative effect resulted from ENTH2-mediated interference with septin assembly pathways. We mapped the ENTH2 determinants responsible for induction of the phenotype and found them to be important for efficient binding to the septin regulatory protein, Bem3. Supporting a physiological role for epsin 2 in cell division, the protein localized to sites of polarized growth and cytokinesis and rescued a defect in cell division induced by Bem3 misregulation. Collectively, our findings provide a potential molecular mechanism linking endocytosis (via epsin 2) with signaling pathways regulating cell division.

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Current awareness on yeast

2008

Yeast

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In order to keep subscribers up‐to‐date with the latest developments in their field, this current awareness service is provided by John Wiley & Sons and contains newly‐published material on yeasts. Each bibliography is divided into 10 sections. 1 Reviews; 2 General; 3 Biochemistry; 4 Biotechnology; 5 Cell Biology; 6 Gene Expression; 7 Genetics; 8 Physiology; 9 Medical Mycology; 10 Recombinant DNA Technology. Within each section, articles are listed in alphabetical order with respect to author. If, in the preceding period, no publications are located relevant to any one of these headings, that section will be omitted. (5 weeks journals ‐ search completed 13th. Aug. 2008)

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Multiple Pathways Regulate Endocytic Coat Disassembly in Saccharomyces cerevisiae for Optimal Downstream Trafficking

Cited by 63 publications

References 32 publications

Role of Scd5, a protein phosphatase-1 targeting protein, in phosphoregulation of Sla1 during endocytosis

Role of Scd5, a protein phosphatase-1 targeting protein, in phosphoregulation of Sla1 during endocytosis

The yeast endocytic protein Epsin 2 functions in a cell-division signaling pathway

Current awareness on yeast

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