A pathway for targeting soluble misfolded proteins to the yeast vacuole.
about
Characterization of an ERAD gene as VPS30/ATG6 reveals two alternative and functionally distinct protein quality control pathways: one for soluble Z variant of human alpha-1 proteinase inhibitor (A1PiZ) and another for aggregates of A1PiZ.Misfolded proteins are sorted by a sequential checkpoint mechanism of ER quality controlAggregation and retention of human urokinase type plasminogen activator in the yeast endoplasmic reticulum.Free-oligosaccharide control in the yeast Saccharomyces cerevisiae: roles for peptide:N-glycanase (Png1p) and vacuolar mannosidase (Ams1p).An HRD/DER-independent ER quality control mechanism involves Rsp5p-dependent ubiquitination and ER-Golgi transportYGR198w (YPP1) targets A30P alpha-synuclein to the vacuole for degradation.Novel genes involved in endosomal traffic in yeast revealed by suppression of a targeting-defective plasma membrane ATPase mutantVacuole biogenesis in Saccharomyces cerevisiae: protein transport pathways to the yeast vacuoleSecretory bulk flow of soluble proteins is efficient and COPII dependentDemonstration in yeast of the function of BP-80, a putative plant vacuolar sorting receptorScreening for stable mutants with amino acid pairs substituted for the disulfide bond between residues 14 and 38 of bovine pancreatic trypsin inhibitor (BPTI).Cellular quality control screening to identify amino acid pairs for substituting the disulfide bonds in immunoglobulin fold domains.Selective processing and metabolism of disease-causing mutant prion proteins.Ubiquitin-mediated targeting of a mutant plasma membrane ATPase, Pma1-7, to the endosomal/vacuolar system in yeastModularity of the Hrd1 ERAD complex underlies its diverse client range.Evasion of endoplasmic reticulum surveillance makes Wsc1p an obligate substrate of Golgi quality controlInterplay of substrate retention and export signals in endoplasmic reticulum quality control.Role of N-oligosaccharide endoplasmic reticulum processing reactions in glycoprotein folding and degradationRicin A chain without its partner B chain is degraded after retrotranslocation from the endoplasmic reticulum to the cytosol in plant cells.Yeast mutants affecting possible quality control of plasma membrane proteins.Control of amino acid permease sorting in the late secretory pathway of Saccharomyces cerevisiae by SEC13, LST4, LST7 and LST8Toward development of a screen to identify randomly encoded, foldable sequences.Secretion of a foreign protein from budding yeasts is enhanced by cotranslational translocation and by suppression of vacuolar targeting.Optimizing recombinant antibodies for intracellular function using hitchhiker-mediated survival selectionExpression of insulin in yeast: the importance of molecular adaptation for secretion and conversion.An endosome-to-plasma membrane pathway involved in trafficking of a mutant plasma membrane ATPase in yeastPolar transmembrane domains target proteins to the interior of the yeast vacuole.Secretory pathway quality control operating in Golgi, plasmalemmal, and endosomal systems.Mutant fibrinogen cleared from the endoplasmic reticulum via endoplasmic reticulum-associated protein degradation and autophagy: an explanation for liver disease.Stress tolerance of misfolded carboxypeptidase Y requires maintenance of protein trafficking and degradative pathwaysRouting misfolded proteins through the multivesicular body (MVB) pathway protects against proteotoxicity.Misfolded proteins traffic from the endoplasmic reticulum (ER) due to ER export signals.The transmembrane domain of acid trehalase mediates ubiquitin-independent multivesicular body pathway sortingDecreased secretion and unfolded protein response upregulation.Hsp70 molecular chaperone facilitates endoplasmic reticulum-associated protein degradation of cystic fibrosis transmembrane conductance regulator in yeast.COOH-terminal truncations promote proteasome-dependent degradation of mature cystic fibrosis transmembrane conductance regulator from post-Golgi compartments.The endosomal protein-sorting receptor sortilin has a role in trafficking α-1 antitrypsinRicin B chain targeted to the endoplasmic reticulum of tobacco protoplasts is degraded by a CDC48- and vacuole-independent mechanism.O-glycosylation as a sorting determinant for cell surface delivery in yeast.ESCRT regulates surface expression of the Kir2.1 potassium channel.
P2860
Q24537406-404F06DD-2F2A-4265-AC84-470965A2ECECQ24677354-F0281E0B-5FD9-4A57-AAF8-1B36AFB42880Q24792861-5DB0424D-1924-4207-AA5A-98DD8B61523DQ27931323-5F4DBC43-E9A9-46D0-B11A-99344E85DA50Q27933526-1E9A557E-61E9-4CB3-9CC5-9EDE83D14535Q27935534-D7C3D231-C2F6-4E46-AE81-9685306A66B5Q27937501-F5652B74-09A9-4AF2-BE04-7CAC47861981Q27938062-230CFF2E-F8DC-4100-BF09-E0523490C416Q28350951-E64B10D6-6BEF-4CB6-86F0-687F7EB3D867Q28361769-8B49E970-6C78-42BE-8BB1-F9AE02EEDCADQ30865816-BAC1BCE0-18D0-456B-A567-BF9492AA47EAQ33214661-5A13143D-F6CC-4143-AA9E-474A1D6A3420Q33471412-AFAB36D8-C633-4EC2-AD92-19282D974D34Q33693280-42401A87-A55F-45CA-AC71-A3ACA68CE038Q33717057-DF361740-C2C2-4CBD-84BC-72B159EDF9E8Q33761462-F2436D06-2DE6-4D55-BB77-4228322967CCQ33769005-3A399742-01D5-4ABF-BC20-6C8B5CF3EFABQ33905603-04DB384B-BB71-4B5D-B593-816AC999ACB6Q33952179-141EDDA2-E25A-4135-8D0F-25045319DCE4Q33957947-24BB14D8-43EA-442F-B3DA-AA8C6B15BD03Q33971473-69752FEA-0184-4201-BE2A-7F0ACB74C9B9Q34067153-737F9FF8-5285-4C47-B6F5-9DFAC8AC0943Q34252124-A184F857-3911-4947-9F3E-A77D8EF244B2Q34313188-4BE18588-5B49-452C-8A1E-D87CE9B62DE7Q34351917-0B9397B1-E1B3-4A71-91F9-762A39CC83C9Q34682524-D5F11037-5DB2-4D19-B903-BBED8FFB4C3EQ34774994-4493F606-A337-4E9C-9731-42DD596157B0Q34970141-A03CED03-AA29-4D95-A5A1-D4A9F87F252DQ35088205-5330A543-5842-4738-ADB3-187A037B8465Q35160985-690AB07E-FFF3-4829-9649-A0C86C1EB42AQ35310258-2019848E-DB09-4796-A2C1-AEEC548ABD31Q35613397-A264CF98-126A-4BAC-B0DC-2877F98EF44BQ35901885-1FC380BA-413D-49B9-B6DC-9A5DE47F6039Q36031460-699BCAE6-67DF-451D-BFC0-F116BE49A2E2Q36280501-B2B524C4-F76F-49F4-8E38-2BD68E40BBEAQ36326371-180F5756-A200-4289-B5A2-B1F35A564CA2Q36466323-B5F1C913-EF0A-41D6-8A0D-4876A5D28C28Q36980987-F7FCCCB2-2A5F-4D6B-8DE6-5D0F49636518Q37220270-DD6BD7D1-DEC5-4602-91DA-D0DEA6165B96Q37473093-F4DA2911-701F-48D8-8B95-5D3C8092B577
P2860
A pathway for targeting soluble misfolded proteins to the yeast vacuole.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
1996年论文
@zh
1996年论文
@zh-cn
name
A pathway for targeting soluble misfolded proteins to the yeast vacuole.
@ast
A pathway for targeting soluble misfolded proteins to the yeast vacuole.
@en
type
label
A pathway for targeting soluble misfolded proteins to the yeast vacuole.
@ast
A pathway for targeting soluble misfolded proteins to the yeast vacuole.
@en
prefLabel
A pathway for targeting soluble misfolded proteins to the yeast vacuole.
@ast
A pathway for targeting soluble misfolded proteins to the yeast vacuole.
@en
P2093
P2860
P356
P1476
A pathway for targeting soluble misfolded proteins to the yeast vacuole.
@en
P2093
P2860
P304
P356
10.1083/JCB.135.3.623
P407
P577
1996-11-01T00:00:00Z