Multiple degradation pathways for misfolded mutants of the yeast plasma membrane ATPase, Pma1.

Multiple degradation pathways for misfolded mutants of the yeast plasma membrane ATPase, Pma1. Research Abstract Details 

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Multiple degradation pathways for misfolded mutants of the yeast plasma membrane ATPase, Pma1. Abstract Text:

Yu Liu,Sujatha Sitaraman,Amy Chang,

To understand protein sorting and quality control in the secretory pathway, we have analyzed intracellular trafficking of the yeast plasma membrane ATPase, Pma1. Pma1 is ideal for such studies because it is a very abundant polytopic membrane protein, and its localization and activity at the plasma membrane are essential for cell viability and growth. We have tested whether the cytoplasmic amino- and carboxyl-terminal domains of Pma1 carry sorting information. As the sole copy of Pma1, mutants truncated at either NH2 or COOH termini are targeted at least partially to the plasma membrane and have catalytic activity to sustain cell viability. The mutants are also delivered to degradative pathways. Strikingly, NH2- and COOH-terminal Pma1 mutants are differentially recognized for degradation at distinct cellular locales. COOH-terminal mutants are recognized for destruction by endoplasmic reticulum-associated degradation. By contrast, NH2-terminal mutants escape detection by endoplasmic reticulum-associated degradation entirely, and undergo endocytosis for vacuolar degradation after apparently normal cell surface targeting. Both NH2- and COOH-terminal mutants are conformationally abnormal, as revealed by increased sensitivity to tryptic cleavage, but are able to assemble to form oligomers. We propose that different quality control mechanisms may assess discrete domains of Pma1 rather than a global conformational state.

Multiple degradation pathways for misfolded mutants of the yeast plasma membrane ATPase, Pma1. Publishing Authors By Initials

Y Liu,S Sitaraman,A Chang,

For similar enzymes and coenzymes: enzymes: hydrolases: peptide hydrolases: endopeptidases: serine endopeptidases: trypsin research abstracts see: enzymes and coenzymes: enzymes: hydrolases: peptide hydrolases: endopeptidases: serine endopeptidases: trypsin research

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Multiple degradation pathways for misfolded mutants of the yeast plasma membrane ATPase, Pma1. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: The Journal of biological chemistry

VOLUME: 281

Page Numbers: 31457-66

Journal Abbreviation: J. Biol. Chem.

ISSN: 0021-9258

DAY: 23

MONTH: 08

YEAR: 2006

Multiple degradation pathways for misfolded mutants of the yeast plasma membrane ATPase, Pma1. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 2985121

Multiple degradation pathways for misfolded mutants of the yeast plasma membrane ATPase, Pma1. Keywords Mesh Terms:

KEYWORDS: Trypsin

MESH TERMS: pharmacology

Chemical & Substance for Abstract: Multiple degradation pathways for misfolded mutants of the yeast plasma membrane ATPase, Pma1. Information

Substance Name: Proton-Translocating ATPases

Registry Number: EC 3.6.3.14

Grant and Affiliation Information for Multiple degradation pathways for misfolded mutants of the yeast plasma membrane ATPase, Pma1.

AFFILIATION: Department of Molecular, Cellular & Developmental Biology, University of Michigan, Ann Arbor, Michigan 48109, USA.

Country: United States

AGENCY: United States NIGMS

GRANT: GM 58212

ACRONYM: GM

MEDLINETA: J Biol Chem

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