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Chapter 7 Analysis of Tyrosine‐Phosphorylated Proteins in Rat Brain Mitochondria.

Authors :
Lewandrowski, Urs
Tibaldi, Elena
Cesaro, Luca
Brunati, Anna M.
Toninello, Antonio
Sickmann, Albert
Salvi, Mauro
Source :
Methods in Enzymology; 2009, Vol. 457, p117-136, 20p
Publication Year :
2009

Abstract

Abstract: Mitochondrial protein phosphorylation is emerging as a central event in mitochondrial signaling. In particular, tyrosine phosphorylation is proving to be an unappreciated mechanism involved in regulation of mitochondrial functions. Tyrosine kinases and phosphatases have been identified in mitochondrial compartments and there is a steadily increasing number of new identified tyrosine‐phosphorylated proteins implicated in a wide spectrum of mitochondrial functions. The deciphering of the tyrosine phoshorylation signaling in mitochondria is strictly linked to the definition of the entire mitochondrial tyrosine phosphoproteome. This chapter describes methods to analyze tyrosine phosphorylation in brain mitochondria: identification of new substrates by biochemical and mass spectrometry approaches and bioinformatic tools to analyze the potential effect of tyrosine phosphorylation on the structure/activity of a protein. [Copyright &y& Elsevier]

Details

Language :
English
ISSN :
00766879
Volume :
457
Database :
Supplemental Index
Journal :
Methods in Enzymology
Publication Type :
Academic Journal
Accession number :
78195699
Full Text :
https://doi.org/10.1016/S0076-6879(09)05007-1