Cdc48-Ufd1-NpI4: Stuck in the middle with Ub

被引：132

作者：

Bays, NW

Hampton, RY

机构：

[1] Exelixis Inc, San Francisco, CA 94080 USA

[2] Univ Calif San Diego, Sect Cell & Dev Biol, Div Biol, La Jolla, CA 92093 USA

来源：

CURRENT BIOLOGY | 2002年 / 12卷 / 10期

关键词：

D O I：

10.1016/S0960-9822(02)00862-X

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The ubiquitin-proteasome pathway has a well-defined beginning and end. Target proteins are initially recognized by upstream components and tagged with polyubiquitin chains. The 26S proteasome then degrades these polyubiquitinated proteins. Until recently, it was not known what, if any, steps occurred between the initial polyubiquitination of target proteins and their final degradation. Several new papers investigating the function of the Cdc48-Ufd1-Np14 complex indicate that there is indeed a middle to the ubiquitin-proteasome pathway. The Cdc48-Ufd1-Np14 complex functions in the recognition of several polyubiquitin-tagged proteins and facilitates their presentation to the 26S proteasome for processive degradation or even more specific processing. The elucidation of Cdc48, Ufd1 and Np14 action not only provides long-sought functions for these specific proteins, but illuminates a poorly understood part of the ubiquitin-proteasome pathway.

引用

收藏

页码：R366 / +

页数：7

相关论文

共 47 条

[1] THE FORMATION OF GOLGI STACKS FROM VESICULATED GOLGI MEMBRANES REQUIRES 2 DISTINCT FUSION EVENTS [J].

ACHARYA, U ;

JACOBS, R ;

PETERS, JM ;

WATSON, N ;

FARQUHAR, MG ;

MALHOTRA, V .

CELL, 1995, 82 (06) :895-904

[2] HRD4/NPL4 is required for the proteasomal processing of ubiquitinated ER proteins [J].

Bays, NW ;

Wilhovsky, SK ;

Goradia, A ;

Hodgkiss-Harlow, K ;

Hampton, RY .

MOLECULAR BIOLOGY OF THE CELL, 2001, 12 (12) :4114-4128

[3] The hydrophobic effect contributes to polyubiquitin chain recognition [J].

Beal, RE ;

Toscano-Cantaffa, D ;

Young, P ;

Rechsteiner, M ;

Pickart, CM .

BIOCHEMISTRY, 1998, 37 (09) :2925-2934

[4] Role of the ubiquitin-selective CDC48UFD1/NPL4 chaperone (segregase) in ERAD of OLE1 and other substrates [J].

Braun, S ;

Matuschewski, K ;

Rape, M ;

Thoms, S ;

Jentsch, S .

EMBO JOURNAL, 2002, 21 (04) :615-621

[5] Genetic analysis of macromolecular transport across the nuclear envelope [J].

Corbett, A ;

Ferrigno, P ;

Henry, M ;

Kahana, J ;

Koepp, D ;

Lee, M ;

Nguyen, L ;

Schlenstedt, G ;

Seedorf, M ;

Shen, E ;

Taura, T ;

Wong, D ;

Silver, P .

EXPERIMENTAL CELL RESEARCH, 1996, 229 (02) :212-216

[6] Valosin-containing protein is a multiubiquitin chain targeting factor required in ubiquitin-proteasome degradation [J].

Dai, RM ;

Li, CCH .

NATURE CELL BIOLOGY, 2001, 3 (08) :740-744

[7] Involvement of valosin-containing protein, an ATPase co-purified with IκBα and 26 S proteasome, in ubiquitin-proteasome-mediated degradation of IκBα [J].

Dai, RM ;

Chen, EY ;

Longo, DL ;

Gorbea, CM ;

Li, CCH .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (06) :3562-3573

[8] Nuclear transport defects and nuclear envelope alterations are associated with mutation of the Saccharomyces cerevisiae NPL4 gene [J].

DeHoratius, C ;

Silver, PA .

MOLECULAR BIOLOGY OF THE CELL, 1996, 7 (11) :1835-1855

[9] THE ATPASE ACTIVITY OF PURIFIED CDC48P FROM SACCHAROMYCES-CEREVISIAE SHOWS COMPLEX DEPENDENCE ON ATP-CONCENTRATION, ADP-CONCENTRATION, AND NADH-CONCENTRATION AND IS COMPLETELY INHIBITED BY NEM [J].

FROHLICH, KU ;

FRIES, HW ;

PETERS, JM ;

MECKE, D .

BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY, 1995, 1253 (01) :25-32

[10] Multiubiquitin chain binding and protein degradation are mediated by distinct domains within the 26 S proteasome subunit Mcb1 [J].

Fu, HY ;

Sadis, S ;

Rubin, DM ;

Glickman, M ;

van Nocker, S ;

Finley, D ;

Vierstra, RD .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (04) :1970-1981

← 1 2 3 4 5 →