Cooperative and independent activities of Sgt2 and Get5 in the targeting of tail-anchored proteins
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Abstract
TPR proteins modulate the activity of molecular chaperones. Here, we describe the S. cerevisiae TPR protein Sgt2 as interaction partner of Ssa1 and Hsp104 and as a component of the GET pathway by interacting with Get5. The GET pathway mediates the sorting of tail-anchored (TA) proteins, harboring a C-terminal trans-membrane segment, to the ER membrane. S. cerevisiae sgt2Δ cells show partial defects in TA protein sorting. Sgt2 activity in vivo relies on its N- and C-terminal domains, whereas the central TPR domain and thus chaperone interactions are dispensable. We show that TA protein sorting defects are more severe in sgt2Δ get5Δ mutants compared to single knockouts. Furthermore, overproduction of Sgt2 becomes toxic to get3Δ but not to get5Δ cells. Together, these findings indicate an additional, Get5-independent role of Sgt2 in TA protein sorting, pointing to parallel pathways of substrate delivery to Get3.
©2011 by Walter de Gruyter Berlin Boston
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Articles in the same Issue
- GENES AND NUCLEIC ACIDS
- Sequence elements outside the catalytic core of natural hairpin ribozymes modulate the reactions differentially
- PROTEIN STRUCTURE AND FUNCTION
- Cooperative and independent activities of Sgt2 and Get5 in the targeting of tail-anchored proteins
- Novel neutrophil inhibitory factor homologue in the buccal gland secretion of Lampetra japonica
- MEMBRANES, LIPIDS, GLYCOBIOLOGY
- Generation of artificial channels by multimerization of β-strands from natural porin
- MOLECULAR MEDICINE
- Gender-related differences in the oxidant state of cells in Fanconi anemia heterozygotes
- CELL BIOLOGY AND SIGNALING
- Mesothelial cells activate the plasma kallikrein-kinin system during pleural inflammation
- Impact of aryl hydrocarbon receptor (AhR) knockdown on cell cycle progression in human HaCaT keratinocytes
- PROTEOLYSIS
- Morpholino knockdown of the ubiquitously expressed transmembrane serine protease TMPRSS4a in zebrafish embryos exhibits severe defects in organogenesis and cell adhesion
- NOVEL TECHNIQUES
- Isolation of dipeptidyl peptidase IV (DP 4) isoforms from porcine kidney by preparative isoelectric focusing to improve crystallization
