Phosphotyrosine: Affecting Locally Acting Globally

Fri, 08/03/2012 - 09:55

Over the past two decades, it has become clear that tyrosine phosphorylation plays a pivotal role in a variety of important signaling pathways in multicellular organisms. In the typical vertebrate cell, phosphotyrosine represents only a tiny fraction of total protein phosphorylation. Yet it is sufficient enough to induce malignant transformation (1), as unregulated phosphotyrosine signaling causes a breakdown in the normal regulation of cellular processes leading to several human diseases (2).

Western Blot: Phosphotyrosine Antibody

The oncogenic signaling pathways driving cell proliferation and survival have been difficult to identify, in part because of the complexity of the pathways and in part because of low cellular levels of tyrosine phosphorylation. Global phospho-proteomic approaches using phosphotyrosine-specific antibodies and tandem mass spectrometry have revealed small numbers of peptides containing phosphotyrosine residues. Several phosphotyrosine sites have been detected in cell systems and cancer cell lines demonstrating the activated signaling networks in diseased states. Tyrosine phosphorylation represents an unusually high proportion (68%) of all phosphorylation in SH3 domains suggesting that tyrosine phosphorylation could also be an important regulatory mechanism for other adaptor domains (3).

  1. PMID: 2561455
  2. PMID: 9426205
  3. PMID: 22615764

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