Review

Nature Reviews Molecular Cell Biology 3, 753-766 (October 2002) | doi:10.1038/nrm934

Furin at the cutting edge: From protein traffic to embryogenesis and disease

Gary Thomas1  About the author

Top

Furin catalyses a simple biochemical reaction — the proteolytic maturation of proprotein substrates in the secretory pathway. But the simplicity of this reaction belies furin's broad and important roles in homeostasis, as well as in diseases ranging from Alzheimer's disease and cancer to anthrax and Ebola fever. This review summarizes various features of furin — its structural and enzymatic properties, intracellular localization, trafficking, substrates, and roles in vivo.

Top

Author affiliations

  1. Vollum Institute, 3181 SW Sam Jackson Park Road, Portland, Oregon 97239, USA.
    Email: thomasg@ohsu.edu
Top
MORE ARTICLES LIKE THIS
These links to content published by NPG are automatically generated

RESEARCH
The crystal structure of the proprotein processing proteinase furin explains its stringent specificity
Nature Structural Biology Article (01 Jul 2003)
Activation of the furin endoprotease is a multiple-step process: requirements for acidification and internal propeptide cleavage
The EMBO Journal Article (01 Apr 1997)
BMP-4 is proteolytically activated by furin and/or PC6 during vertebrate embryonic development
The EMBO Journal Article (17 Aug 1998)
The phosphorylation state of an autoregulatory domain controls PACS-1-directed protein traffic
The EMBO Journal Article (01 Dec 2003)
PACS-1 binding to adaptors is required for acidic cluster motif-mediated protein traffic
The EMBO Journal Article (01 May 2001)
See all 7 matches for Research

Extra navigation

Subscribe

Subscribe to Nature Reviews Molecular Cell Biology

Search PubMed for

Open Innovation Challenges

naturejobs

More science jobs
Post a job for free

Advertisement