<i>SPO71</i>
            Encodes a Developmental Stage-Specific Partner for Vps13 in Saccharomyces cerevisiae

Park, Jae-Sook; Okumura, Yuuya; Tachikawa, Hiroyuki; Neiman, Aaron M.

doi:10.1128/ec.00239-13

Cited by 48 publications

(76 citation statements)

References 31 publications

(53 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…We see that ama1D cells make rounded PSMs that retain bright Don1-GFP puncta ( Figure 6D, right) as previously shown (Diamond et al 2009;Park et al 2013), at a frequency similar to what was observed in the sps1D and spo77D mutants (Table 1; P-value ,0.0001). We also observe hyperelongated PSMs in ama1D cells ( Figure 6D, left), consistent with previous reports (Diamond et al 2009).…”

Section: Sps1 Has a Dynamic Localization During Sporulationsupporting

confidence: 85%

Timely Closure of the Prospore Membrane Requires SPS1 and SPO77 in Saccharomyces cerevisiae

et al. 2016

View full text Add to dashboard Cite

During sporulation in Saccharomyces cerevisiae, a double lipid bilayer called the prospore membrane is formed de novo, growing around each meiotic nucleus and ultimately closing to create four new cells within the mother cell. Here we show that SPS1, which encodes a kinase belonging to the germinal center kinase III family, is involved in prospore membrane development and is required for prospore membrane closure. We find that SPS1 genetically interacts with SPO77 and see that loss of either gene disrupts prospore membrane closure in a similar fashion. Specifically, cells lacking SPS1 and SPO77 produce hyperelongated prospore membranes from which the leading edge protein complex is not removed from the prospore membrane in a timely fashion. The SPS1/ SPO77 pathway is required for the proper phosphorylation and stability of Ssp1, a member of the leading edge protein complex that is removed and degraded when the prospore membrane closes. Genetic dissection of prospore membrane closure finds SPS1 and SPO77 act in parallel to a previously described pathway of prospore membrane closure that involves AMA1, an activator of the meiotic anaphase promoting complex.KEYWORDS prospore membrane; meiotic exit; anaphase promoting complex; sporulation; cytokinesis; germinal center kinase B IOLOGICAL membranes provide a barrier for inhibiting the flow of materials between a cell and its surroundings and for compartmentalizing the contents of the various organelles within a cell. The size and shape of membranes are central to their functions. Membranes are essential for many fundamental cellular processes including ion balance, energy generation, and secretion. In cell division, membrane dynamics are particularly important, where they act to segregate the contents of the cellular progeny.The process of cell division differs among cells. Most commonly, animal cells divide through a mechanism requiring the assembly of an actin-based contractile ring at the division site (reviewed in Green et al. 2012). This actomyosin ring contracts and matures, ultimately leading to scission of the membrane necks mediated by the ESCRTIII (endosomal sorting complex required for transport III) complex. However, other variations of cytokinesis occur: cellularization during early Drosophila embryogenesis, which requires the growth of membranes around the nuclei before the contractile event (Lee and Harris 2014) and cell division in plants, which requires the secretion of vesicles to the division plane to form the phragmoplast, which will eventually separate the two daughter cells (reviewed in Jürgens 2005). Actin is not always involved in cytokinesis; although prokaryotic cells have actin-like filaments (reviewed in Carballido-López 2006), these filaments are not used for cytokinesis (Pollard and Wu 2010). Similarly, cytokinesis in Trypanosoma brucei (a bikont eukaryote) does not require actin but seems to utilize microtubules (Wheeler et al. 2013). In the budding yeast Saccharomyces cerevisiae, an actin-based contractile ring plays a role in ...

show abstract

Section: Sps1 Has a Dynamic Localization During Sporulationsupporting

confidence: 85%

Timely Closure of the Prospore Membrane Requires SPS1 and SPO77 in Saccharomyces cerevisiae

et al. 2016

View full text Add to dashboard Cite

show abstract

“…More specifically, the yeast vps13Δ cells show a depletion of PtdIns4P levels in prospore membranes. 26,39 Distinct PtdIns-phosphates play essential roles in autophagy at different levels. For example, PtdIns(3,4,5)P 3 is essential for the signaling pathway that regulates TORC1 (TOR complex 1), and PtdIns(4,5)P 2 is required for the formation of autophagosomes originated from the plasma membrane.…”

Section: Discussionmentioning

confidence: 99%

TipC and the chorea-acanthocytosis protein VPS13A regulate autophagy inDictyosteliumand human HeLa cells

2015

View full text Add to dashboard Cite

Deficient autophagy causes a distinct phenotype in Dictyostelium discoideum, characterized by the formation of multitips at the mound stage. This led us to analyze autophagy in a number of multitipped mutants described previously (tipA(-), tipB(-), tipC(-), and tipD(-)). We found a clear autophagic dysfunction in tipC(-) and tipD(-) while the others showed no defects. tipD codes for a homolog of Atg16, which confirms the role of this protein in Dictyostelium autophagy and validates our approach. The tipC-encoded protein is highly similar to human VPS13A (also known as chorein), whose mutations cause the chorea-acanthocytosis syndrome. No member of the VPS13 protein family has been previously related to autophagy despite the presence of a region of similarity to Atg2 at the C terminus. This region also contains the conserved domain of unknown function DUF1162. Of interest, the expression of the TipC C-terminal coding sequence containing these 2 motifs largely complemented the mutant phenotype. Dictyostelium cells lacking TipC displayed a reduced number of autophagosomes visualized with the markers GFP-Atg18 and GFP-Atg8 and an impaired autophagic degradation as determined by a proteolytic cleavage assay. Downregulation of human VPS13A in HeLa cells by RNA interference confirmed the participation of the human protein in autophagy. VPS13A-depleted cells showed accumulation of autophagic markers and impaired autophagic flux.

show abstract

“…Moreover, after loss of Vps13p function an in increased cytotoxicity of an expanded polyQ domain in Rnq1p has been detected (10). Recently, Vps13p was shown to be required for prospore membrane morphogenesis through regulation of phosphatidylinositol phosphatases (11,12). Our previous results have established the 450 kDa protein COH1 as an atypical Golgi matrix protein lacking coiled-coil domains that is crucial for Golgi complex organization.…”

mentioning

confidence: 82%

Cohen Syndrome-associated Protein COH1 Physically and Functionally Interacts with the Small GTPase RAB6 at the Golgi Complex and Directs Neurite Outgrowth

Seifert

Kühnisch

Maritzen

et al. 2015

Journal of Biological Chemistry

View full text Add to dashboard Cite

Background: COH1 is a peripheral membrane protein that is required for Golgi complex integrity and function. Results: Association of COH1 with the Golgi complex is mediated by its interaction with RAB6 and is required for neurite outgrowth. Conclusion: COH1 acts as downstream effector protein of RAB6. Significance: Defective neuronal outgrowth due to loss of COH1 contributes to the neurological impairments found in Cohen syndrome patients.

show abstract

SPO71 Encodes a Developmental Stage-Specific Partner for Vps13 in Saccharomyces cerevisiae

Cited by 48 publications

References 31 publications

Timely Closure of the Prospore Membrane Requires SPS1 and SPO77 in Saccharomyces cerevisiae

Timely Closure of the Prospore Membrane Requires SPS1 and SPO77 in Saccharomyces cerevisiae

TipC and the chorea-acanthocytosis protein VPS13A regulate autophagy inDictyosteliumand human HeLa cells

Cohen Syndrome-associated Protein COH1 Physically and Functionally Interacts with the Small GTPase RAB6 at the Golgi Complex and Directs Neurite Outgrowth

Contact Info

Product

Resources

About