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Books > Science & Mathematics > Biology, life sciences > Biochemistry > Proteins
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The Small GTPase Ran (Hardcover, 2001 ed.)
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The Small GTPase Ran (Hardcover, 2001 ed.)
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RAN: AN ATYPICAL GTPASE Mark G. Rush and Peter D'Eustachio New York
University School o/Medicine. Department,o/Biochemistry New York NY
10016 ABSTRACT GTPases, proteins that bind and hydrolyze GTP
(guanosine triphos- phate) are critical regulators of many
metabolic pathways. Although these proteins are enzymes that
catalyze the hydrolysis of GTP to GDP + Pi, their primary function
is not the hydrolysis of GTP per se, but rather the coupling of
this hydrolysis to metabolic regulation. Such coupling is gen-
erally achieved through the interaction of the GTP-bound form of
the GTPase with proteins known as *effectors. Effectors are often
enzymes whose activities are modulated by the GTPase. However,
effectors can also be structural proteins involved in assembling
intracellular macromo- lecular complexes, such as actin filaments
and microtubules, as well as proteins involved in the intracellular
transport of proteins and RNAs. In- deed, the subject of this
anthology, the small GTPase Ran, may exert most or all of its
regulatory functions by interacting with non-enzyme effectors. This
property of Ran distinguishes it from other well studied GTPases,
and has resulted in the elucidation of novel mechanisms of Ran
action that are quite distinct from previously established
paradigms of GTPase function. 1. INTRODUCTION The Ras-related
nuclear protein Ran is a highly conserved (80% identity among
yeasts and humans) member of the Ras superfamily of small GTP
binding and hydrolyzing proteins.
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