scholarly journals The Adaptor Complex AP-4 Regulates Vacuolar Protein Sorting at the trans-Golgi Network by Interacting with VACUOLAR SORTING RECEPTOR1

2015 ◽  
Vol 170 (1) ◽  
pp. 211-219 ◽  
Author(s):  
Kentaro Fuji ◽  
Makoto Shirakawa ◽  
Yuki Shimono ◽  
Tadashi Kunieda ◽  
Yoichiro Fukao ◽  
...  
Keyword(s):  
Protein Sorting ◽  
Vacuolar Protein Sorting ◽  
Trans Golgi Network ◽  
Vacuolar Sorting ◽  
Vacuolar Protein ◽  
Golgi Network

scholarly journals CONTINUOUS VASCULAR RING (COV1) is a trans-Golgi Network-Localized Membrane Protein Required for Golgi Morphology and Vacuolar Protein Sorting

2014 ◽  
Vol 55 (4) ◽  
pp. 764-772 ◽  
Author(s):  
Makoto Shirakawa ◽  
Haruko Ueda ◽  
Yasuko Koumoto ◽  
Kentaro Fuji ◽  
Chiaki Nishiyama ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Protein Sorting ◽  
Vascular Ring ◽  
Vacuolar Protein Sorting ◽  
Trans Golgi Network ◽  
Vacuolar Protein ◽  
Golgi Network

scholarly journals Synthetic Genetic Interactions With Temperature-Sensitive Clathrin in Saccharomyces cerevisiae: Roles for Synaptojanin-Like Inp53p and Dynamin-Related Vps1p in Clathrin-Dependent Protein Sorting at the trans-Golgi Network

Genetics ◽  
2000 ◽  
Vol 154 (1) ◽  
pp. 83-97
Author(s):  
Eric S Bensen ◽  
Giancarlo Costaguta ◽  
Gregory S Payne
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Molecular Mechanisms ◽  
Protein Transport ◽  
Protein Sorting ◽  
Genetic Interactions ◽  
Carboxypeptidase Y ◽  
Temperature Sensitive ◽  
Trans Golgi Network ◽  
Vacuolar Protein ◽  
Golgi Network

Abstract Clathrin is involved in selective protein transport at the Golgi apparatus and the plasma membrane. To further understand the molecular mechanisms underlying clathrin-mediated protein transport pathways, we initiated a genetic screen for mutations that display synthetic growth defects when combined with a temperature-sensitive allele of the clathrin heavy chain gene (chc1-521) in Saccharomyces cerevisiae. Mutations, when present in cells with wild-type clathrin, were analyzed for effects on mating pheromone α-factor precursor maturation and sorting of the vacuolar protein carboxypeptidase Y as measures of protein sorting at the yeast trans-Golgi network (TGN) compartment. By these criteria, two classes of mutants were obtained, those with and those without defects in protein sorting at the TGN. One mutant with unaltered protein sorting at the TGN contains a mutation in PTC1, a type 2c serine/threonine phosphatase with widespread influences. The collection of mutants displaying TGN sorting defects includes members with mutations in previously identified vacuolar protein sorting genes (VPS), including the dynamin family member VPS1. Striking genetic interactions were observed by combining temperature-sensitive alleles of CHC1 and VPS1, supporting the model that Vps1p is involved in clathrin-mediated vesicle formation at the TGN. Also in the spectrum of mutants with TGN sorting defects are isolates with mutations in the following: RIC1, encoding a product originally proposed to participate in ribosome biogenesis; LUV1, encoding a product potentially involved in vacuole and microtubule organization; and INP53, encoding a synaptojanin-like inositol polyphosphate 5-phosphatase. Disruption of INP53, but not the related INP51 and INP52 genes, resulted in α-factor maturation defects and exacerbated α-factor maturation defects when combined with chc1-521. Our findings implicate a wide variety of proteins in clathrin-dependent processes and provide evidence for the selective involvement of Inp53p in clathrin-mediated protein sorting at the TGN.

scholarly journals Trafficking of Vacuolar Proteins: The Crucial Role of Arabidopsis Vacuolar Protein Sorting 29 in Recycling Vacuolar Sorting Receptor

2012 ◽  
Vol 24 (12) ◽  
pp. 5058-5073 ◽  
Author(s):  
Hyangju Kang ◽  
Soo Youn Kim ◽  
Kyungyoung Song ◽  
Eun Ju Sohn ◽  
Yongjik Lee ◽  
...  
Keyword(s):  
Crucial Role ◽  
Protein Sorting ◽  
Vacuolar Protein Sorting ◽  
Vacuolar Sorting Receptor ◽  
Vacuolar Sorting ◽  
Sorting Receptor ◽  
Vacuolar Protein

scholarly journals An Interorganellar Bidding War: Vps13 Localization by Competitive Organelle-Specific Adaptors

Contact ◽  
2018 ◽  
Vol 1 ◽  
pp. 251525641881462
Author(s):  
Samantha K. Dziurdzik ◽  
Björn D.M. Bean ◽  
Elizabeth Conibear
Keyword(s):  
Endoplasmic Reticulum ◽  
Recent Work ◽  
Protein Sorting ◽  
Repeat Region ◽  
Vacuolar Protein Sorting ◽  
Membrane Contact Sites ◽  
Contact Sites ◽  
Prospore Membrane ◽  
Membrane Contact ◽  
Vacuolar Protein

Membrane contact sites are regulated through the controlled recruitment of constituent proteins. Yeast vacuolar protein sorting 13 (Vps13) dynamically localizes to membrane contact sites at endosomes, vacuoles, mitochondria, and the endoplasmic reticulum under different cellular conditions and is recruited to the prospore membrane during meiosis. Prior to our recent work, the mechanism for localization at contact sites was largely unknown. We identified Ypt35 as a novel Vps13 adaptor for endosomes and the nucleus-vacuole junction. Furthermore, we discovered a conserved recruitment motif in Ypt35 and found related motifs in the prospore membrane and mitochondrial adaptors, Spo71 and Mcp1, respectively. All three adaptors compete for binding to a six-repeat region of Vps13, suggesting adaptor competition regulates Vps13 localization. Here, we summarize and discuss the implications of our work, highlighting key outstanding questions.

MP005INCREASED LYSOSOMAL DEGRADATION OF AQP2 IN MPKCCDC14 CELLS WITH KNOCKDOWN OF VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 35

2016 ◽  
Vol 31 (suppl_1) ◽  
pp. i345-i345
Author(s):  
Hyo-Jung Choi ◽  
Mi Suk Lee ◽  
Dasom Kim ◽  
Eui-Jung Park ◽  
Yu-Jung Lee ◽  
...  
Keyword(s):  
Protein Sorting ◽  
Lysosomal Degradation ◽  
Vacuolar Protein Sorting ◽  
Vacuolar Protein
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