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Farnesylated proteins: how do they get to where they need to go, and how does location regulate their ability to control proliferation, death, transformation and aging?
Author(s) -
Cox Adrienne D.,
Madigan James P.,
Fiordalisi James J.,
Der Channing J.,
Berzat Anastacia C.,
Philips Mark R.,
Bivona Trever,
Ahearn Ian,
Quatela Steven,
Capell Brian C.,
Erdos Michael R.,
Gordon Leslie B.,
Varga Renee,
Collins Francis S.
Publication year - 2006
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.20.5.a852-c
Subject(s) - microbiology and biotechnology , gtpase , internalization , small gtpase , biology , prenylation , ubiquitin , chemistry , signal transduction , biochemistry , cell , gene , enzyme
Ras and Rho family small GTPases require post‐translational modification by isoprenoid lipids in order to localize correctly within the cell and to transmit the signals that regulate normal cellular homeostasis or oncogenesis. In addition, the location and function of some Ras and Rho proteins can be regulated by a farnesyl‐phosphate switch that results in loss of plasma membrane binding and transition from a proliferative signal to a death signal, or vice versa. Other small GTPases undergo regulation by a lipid‐ubiquitin switch for internalization. Finally, the loss of a specific proteolytic cleavage site in Progerin, a mutant form of nuclear LaminA protein associated with premature aging, results both in inappropriate retention of the farnesyl group and in inappropriate nuclear localization and structural dysfunction. How location dictates the functions of these proteins will be discussed.