| pubmed-article:11481477 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11481477 | lifeskim:mentions | umls-concept:C0007603 | lld:lifeskim |
| pubmed-article:11481477 | lifeskim:mentions | umls-concept:C0699040 | lld:lifeskim |
| pubmed-article:11481477 | lifeskim:mentions | umls-concept:C0001473 | lld:lifeskim |
| pubmed-article:11481477 | lifeskim:mentions | umls-concept:C0596988 | lld:lifeskim |
| pubmed-article:11481477 | lifeskim:mentions | umls-concept:C0205360 | lld:lifeskim |
| pubmed-article:11481477 | lifeskim:mentions | umls-concept:C2700289 | lld:lifeskim |
| pubmed-article:11481477 | pubmed:issue | 16 | lld:pubmed |
| pubmed-article:11481477 | pubmed:dateCreated | 2001-8-1 | lld:pubmed |
| pubmed-article:11481477 | pubmed:abstractText | Pma1 is a plasma membrane H(+)-ATPase whose activity at the cell surface is essential for cell viability. In this paper we describe a temperature-sensitive pma1 allele, pma1-10 (with two point mutations in the first cytoplasmic loop of Pma1), in which the newly synthesized mutant protein fails to remain stable at the cell surface at 37 degrees C. Instead, Pma1-10 appears to undergo internalization for vacuolar degradation in a manner dependent on End4, Vps27, Doa4, and Pep4. By contrast with wild-type Pma1, mutant Pma1-10 is hypophosphorylated and fails to associate with a Triton-insoluble fraction at 37 degrees C, suggesting failure to enter lipid rafts. Kinetic analysis reveals that, at the permissive temperature, newly synthesized Pma1-10 acquires Triton-insolubility before becoming stabilized. We suggest that phosphorylation and lipid raft association may play important roles in maintaining protein stability at the plasma membrane. | lld:pubmed |
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| pubmed-article:11481477 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:11481477 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:11481477 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11481477 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:11481477 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:11481477 | pubmed:author | pubmed-author:ChangAA | lld:pubmed |
| pubmed-article:11481477 | pubmed:author | pubmed-author:GonyJJ | lld:pubmed |
| pubmed-article:11481477 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11481477 | pubmed:day | 31 | lld:pubmed |
| pubmed-article:11481477 | pubmed:volume | 98 | lld:pubmed |
| pubmed-article:11481477 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11481477 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11481477 | pubmed:pagination | 9104-9 | lld:pubmed |
| pubmed-article:11481477 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:11481477 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11481477 | pubmed:articleTitle | A mutant plasma membrane ATPase, Pma1-10, is defective in stability at the yeast cell surface. | lld:pubmed |
| pubmed-article:11481477 | pubmed:affiliation | Departments of Anatomy and Structural Biology, and Developmental and Molecular Biology, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA. | lld:pubmed |
| pubmed-article:11481477 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11481477 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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