The yeast ubiquitin ligase Rsp5 downregulates the alpha subunit of nascent polypeptide-associated complex Egd2 under stress conditions
نویسندگان
چکیده
منابع مشابه
Nascent polypeptide-associated complex stimulates protein import into yeast mitochondria.
To identify yeast cytosolic proteins that mediate targeting of precursor proteins to mitochondria, we developed an in vitro import system consisting of purified yeast mitochondria and a radiolabeled mitochondrial precursor protein whose C terminus was still attached to the ribosome. In this system, the N terminus of the nascent chain was translocated across both mitochondrial membranes, generat...
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Sla1 and Rvs167 are yeast proteins required for receptor internalization and organization of the actin cytoskeleton. Here we provide evidence that Sla1 and Rvs167 are orthologues of the mammalian CIN85 and endophilin proteins, respectively, which are required for ligand-stimulated growth factor receptor internalization. Sla1 is similar in domain structure to CIN85 and binds directly to the endo...
متن کاملThe role of Rsp5 ubiquitin ligase in regulation of diverse processes in yeast cells.
Rsp5 is a conserved ubiquitin ligase involved in regulation of numerous cellular processes. A growing number of publications describing new functions of the ligase have appeared in recent years. Rsp5 was shown to be involved in the control of intracellular trafficking of proteins via endocytosis and multivesicular body sorting. Moreover, nuclear functions of Rsp5 in response to various stresses...
متن کاملIdentification of the endocytic sorting signal recognized by the Art1-Rsp5 ubiquitin ligase complex
Targeted endocytosis of plasma membrane (PM) proteins allows cells to adjust their complement of membrane proteins to changing extracellular conditions. For a wide variety of PM proteins, initiation of endocytosis is triggered by ubiquitination. In yeast, arrestin-related trafficking adaptors (ARTs) enable a single ubiquitin ligase, Rsp5, to specifically and selectively target a wide range of P...
متن کاملG Protein Mono-ubiquitination by the Rsp5 Ubiquitin Ligase.
Emerging evidence suggests that ubiquitination serves as a protein trafficking signal in addition to its well characterized role in promoting protein degradation. The yeast G protein alpha subunit Gpa1 represents a rare example of a protein that undergoes both mono- and poly-ubiquitination. Whereas mono-ubiquitinated Gpa1 is targeted to the vacuole, poly-ubiquitinated Gpa1 is directed instead t...
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ژورنال
عنوان ژورنال: FEBS Journal
سال: 2009
ISSN: 1742-464X
DOI: 10.1111/j.1742-4658.2009.07226.x