The Small GTPase Ran

Peter D'Eustachio

ISBN 10: 0792375106 / ISBN 13: 9780792375104

Published by Springer US, Springer New York Sep 2001, 2001

About this Item

This item is printed on demand - it takes 3-4 days longer - Neuware -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. 244 pp. Englisch.

Seller Inventory # 9780792375104

Bibliographic Details

• Title: The Small GTPase Ran
• Publisher: Springer US, Springer New York Sep 2001
• Publication Date: 2001
• Language: English
• ISBN 10: 0792375106
• ISBN 13: 9780792375104
• Binding: Buch
• Condition: Neu
• Dimensions: 241W x 160H x 18D millimeters 241 millimeters width by 160 millimeters height by 18 millimeters depth
• Weight: 535 grams

About this title

Synopsis

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.

Synopsis

The Ras-related nuclear protein Ran is a member of the so-called Ras-superfamily of small GTP-binding proteins and hydrolyzing proteins. A variety of edited anthologies related to the Ras-superfamily have appeared over the last decade, but Ran has been under-represented in all of them. This under-representation is not due to the fact that Ran is unimportant or non-abundant. It is almost certainly because Ran was discovered and its functions elucidated only recently, and that some of these functions may not follow the typical Ras-superfamily paradign. Even workers in the field have difficulty keeping up with the Ran literature, and most outsiders rarely try even though they may be aware that major breakthroughs regarding the mechanisms of nuclear-cytosolic transport, mitosis and the maintenance of nuclear structure have depended upon an understanding of Ran function."The Small GTPase Ran" is meant to provide specialists with a concise summary of some of the recent research in this area, along with background describing its initial identification and early characterization.