Characterization of AND-34 Function and Signaling

Kyriacos Felekkis, Lawrence Quilliam, Adam Lerner

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

AND-34 is a member of a novel family of proteins (NSP1, NSP2, and NSP3) that have an amino-terminal SH2 domain but bind by a carboxy-terminal GEF (Cdc25)-like domain to the carboxy-terminus of the focal adhesion adapter protein p130Cas. Direct GEF activity of AND-34 toward Ras subfamily members has not been demonstrated with purified protein. Overexpression of AND-34 in epithelial breast cancer cells leads to activation of Rac and Cdc42 by a PI3K-dependent mechanism. This chapter will describe the techniques we used to examine AND-34-induced Rac, Cdc42, Akt, and PAK1 activation in human breast cancer cell lines and in murine lymphoid cell lines. In addition, we summarize techniques used to determine that AND-34 overexpression does not activate R-Ras in MCF-7 cells.

Original languageEnglish
Pages (from-to)55-63
Number of pages9
JournalMethods in Enzymology
Volume407
DOIs
StatePublished - 2005
Externally publishedYes

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Crk-Associated Substrate Protein
Cells
Breast Neoplasms
Cell Line
Focal Adhesions
src Homology Domains
MCF-7 Cells
Chemical activation
Phosphatidylinositol 3-Kinases
Proteins
Lymphocytes
Adhesion

ASJC Scopus subject areas

  • Biochemistry

Cite this

Characterization of AND-34 Function and Signaling. / Felekkis, Kyriacos; Quilliam, Lawrence; Lerner, Adam.

In: Methods in Enzymology, Vol. 407, 2005, p. 55-63.

Research output: Contribution to journalArticle

Felekkis, Kyriacos ; Quilliam, Lawrence ; Lerner, Adam. / Characterization of AND-34 Function and Signaling. In: Methods in Enzymology. 2005 ; Vol. 407. pp. 55-63.
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