Analysis of function and regulation of proteins that mediate signal transduction by use of lipid-modified plasma membrane-targeting sequences

Gary W. Reuther, Janice E. Buss, Lawrence Quilliam, Geoffrey J. Clark, Channing J. Der

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

It is now established that the function of many signaling molecules is controlled, in part, by regulation of subcellular localization. For example, the dynamic recruitment of normally cytosolic proteins to the plasma membrane, by activated Ras or activated receptor tyrosine kinases, facilitates their interaction with other membrane-associated components that participate in their full activation (e.g., Raf-1). Therefore, the creation of chimeric proteins that contain lipid-modified signaling sequences that direct membrane localization allows the generation of constitutively activated variants of such proteins. The amino-terminal myristoylation signal sequence of Src family proteins and the carboxy-terminal prenylation signal sequence of Ras proteins have been widely used to achieve this goal. Such membrane-targeted variants have proved to be valuable reagents in the study of the biochemical and biological properties of many signaling molecules.

Original languageEnglish (US)
Pages (from-to)331-350
Number of pages20
JournalMethods in Enzymology
Volume327
DOIs
StatePublished - 2000
Externally publishedYes

Fingerprint

Signal transduction
Cell membranes
Signal Transduction
Cell Membrane
Lipids
Protein Sorting Signals
Membranes
Proteins
Prenylation
ras Proteins
Molecules
Receptor Protein-Tyrosine Kinases
Chemical activation

ASJC Scopus subject areas

  • Biochemistry

Cite this

Analysis of function and regulation of proteins that mediate signal transduction by use of lipid-modified plasma membrane-targeting sequences. / Reuther, Gary W.; Buss, Janice E.; Quilliam, Lawrence; Clark, Geoffrey J.; Der, Channing J.

In: Methods in Enzymology, Vol. 327, 2000, p. 331-350.

Research output: Contribution to journalArticle

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