Literature DB >> 1485954

Protein prenylation: more than just glue?

A D Cox1, C J Der.   

Abstract

As with other lipid modifications of proteins, prenylation now appears to be critically important in the regulation of protein function. Recent research has led to an explosion of information concerning prenylation signals, prenyl transferase enzymes and the role of prenylation in protein-membrane interactions. Experiments have examined the role of prenylation in protein function and the results suggest that protein prenylation may be involved in facilitating proper subcellular localization, promoting protein-protein and protein-membrane interactions and regulating protein function.

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Year:  1992        PMID: 1485954     DOI: 10.1016/0955-0674(92)90133-w

Source DB:  PubMed          Journal:  Curr Opin Cell Biol        ISSN: 0955-0674            Impact factor:   8.382


  51 in total

Review 1.  Rho GTPases and their effector proteins.

Authors:  A L Bishop; A Hall
Journal:  Biochem J       Date:  2000-06-01       Impact factor: 3.857

2.  Acylation stabilizes a protease-resistant conformation of protoporphyrinogen oxidase, the molecular target of diphenyl ether-type herbicides.

Authors:  S Arnould; M Takahashi; J M Camadro
Journal:  Proc Natl Acad Sci U S A       Date:  1999-12-21       Impact factor: 11.205

3.  RhoA biological activity is dependent on prenylation but independent of specific isoprenoid modification.

Authors:  Patricia A Solski; Whitney Helms; Patricia J Keely; Lishan Su; Channing J Der
Journal:  Cell Growth Differ       Date:  2002-08

4.  Multiple sequence elements facilitate Chp Rho GTPase subcellular location, membrane association, and transforming activity.

Authors:  Emily J Chenette; Natalia Y Mitin; Channing J Der
Journal:  Mol Biol Cell       Date:  2006-04-26       Impact factor: 4.138

5.  Rho2 is a target of the farnesyltransferase Cpp1 and acts upstream of Pmk1 mitogen-activated protein kinase signaling in fission yeast.

Authors:  Yan Ma; Takayoshi Kuno; Ayako Kita; Yuta Asayama; Reiko Sugiura
Journal:  Mol Biol Cell       Date:  2006-09-27       Impact factor: 4.138

6.  An experimentally derived database of candidate Ras-interacting proteins.

Authors:  Lawrence E Goldfinger; Celeste Ptak; Erin D Jeffery; Jeffrey Shabanowitz; Jaewon Han; Jacob R Haling; Nicholas E Sherman; Jay W Fox; Donald F Hunt; Mark H Ginsberg
Journal:  J Proteome Res       Date:  2007-04-17       Impact factor: 4.466

7.  Spreading of differentiating human monocytes is associated with a major increase in membrane-bound CDC42.

Authors:  M Aepfelbacher; F Vauti; P C Weber; J A Glomset
Journal:  Proc Natl Acad Sci U S A       Date:  1994-05-10       Impact factor: 11.205

8.  Structural Dynamics in Ras and Related Proteins upon Nucleotide Switching.

Authors:  Rane A Harrison; Jia Lu; Martin Carrasco; John Hunter; Anuj Manandhar; Sudershan Gondi; Kenneth D Westover; John R Engen
Journal:  J Mol Biol       Date:  2016-10-14       Impact factor: 5.469

Review 9.  Aberrant function of the Ras signal transduction pathway in human breast cancer.

Authors:  G J Clark; C J Der
Journal:  Breast Cancer Res Treat       Date:  1995-07       Impact factor: 4.872

10.  NMR studies of novel inhibitors bound to farnesyl-protein transferase.

Authors:  K S Koblan; J C Culberson; S J Desolms; E A Giuliani; S D Mosser; C A Omer; S M Pitzenberger; M J Bogusky
Journal:  Protein Sci       Date:  1995-04       Impact factor: 6.725

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