Mitochondrial tyrosine phosphoproteome: new insights from an up-to-date analysis

Biofactors. 2010 Nov-Dec;36(6):437-50. doi: 10.1002/biof.123.

Abstract

Tyrosine phosphorylation is a newcomer in the mitochondrial signaling and is currently emerging as an important mechanism for regulating mitochondrial processes. But to what extent? By analyzing an updated draft of the mitochondrial tyrosine phosphoproteome, the following observations can be drawn: more than a hundred mitochondrial proteins undergo tyrosine phosphorylation, phosphotyrosine proteins are distributed in each of the submitochondrial compartments, and mitochondrial tyrosine phosphorylated proteins are involved in a variety of functions as metabolism (electron transport chain, Krebs cycle, fatty acid and amino acid metabolism), solute and protein transport, mitochondrial translation machinery, quality protein assessment, oxidative stress, apoptosis, fission, and other. This large and varied collection suggests that tyrosine phosphorylation could be a widespread mechanism in modulating mitochondrial functions. Moreover the in silico model is here used to explore potential effects of tyrosine phosphorylation on selected mitochondrial proteins pointing out some future perspectives in this field.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Humans
  • Mitochondria / metabolism*
  • Mitochondrial Proteins* / chemistry
  • Mitochondrial Proteins* / classification
  • Mitochondrial Proteins* / metabolism
  • Models, Molecular
  • Phosphoproteins* / chemistry
  • Phosphoproteins* / classification
  • Phosphoproteins* / metabolism
  • Phosphorylation
  • Phosphotransferases / metabolism*
  • Proteome / metabolism*
  • Tyrosine* / chemistry
  • Tyrosine* / metabolism

Substances

  • Mitochondrial Proteins
  • Phosphoproteins
  • Proteome
  • Tyrosine
  • Phosphotransferases