PCI Complexes: Beyond the Proteasome, CSN, and eIF3 Troika

Elah Pick; Kay Hofmann; Michael Glickman

doi:10.1016/j.molcel.2009.07.009

PCI Complexes: Beyond the Proteasome, CSN, and eIF3 Troika

Elah Pick, Kay Hofmann, Michael Glickman

Research output: Contribution to journal › Short survey › peer-review

Abstract

The bipartite PCI domain serves as the principal scaffold for proteasome lid, CSN, and eIF3, complexes that influence protein life span. PCI domains are also found in newly identified complexes directing nucleic acid regulation. The breadth of functions associated with the extended PCI family is a factor of shared subunits, among them a common factor Sem1/DSS1 that facilitates complex assembly.

Original language	English
Pages (from-to)	260-264
Number of pages	5
Journal	Molecular Cell
Volume	35
Issue number	3
DOIs	https://doi.org/10.1016/j.molcel.2009.07.009
State	Published - 14 Aug 2009

ASJC Scopus subject areas

Molecular Biology
Cell Biology

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10.1016/j.molcel.2009.07.009

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abstract = "The bipartite PCI domain serves as the principal scaffold for proteasome lid, CSN, and eIF3, complexes that influence protein life span. PCI domains are also found in newly identified complexes directing nucleic acid regulation. The breadth of functions associated with the extended PCI family is a factor of shared subunits, among them a common factor Sem1/DSS1 that facilitates complex assembly.",

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PCI Complexes: Beyond the Proteasome, CSN, and eIF3 Troika

Abstract

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