Global phosphotyrosinylated protein profile of cell-matrix adhesion complexes of trabecular meshwork cells.

Journal Article (Journal Article)

Dysregulation of the mechanical properties and cell adhesive interactions of trabecular meshwork (TM) are known to impair aqueous humor drainage and elevate intraocular pressure in glaucoma patients. The identity of regulatory mechanisms underlying TM mechanotransduction, however, remains elusive. Here we analyzed the phosphotyrosine proteome of human TM cell-extracellular matrix (ECM) adhesion complexes, which play a key role in sensing and transducing extracellular chemical and mechanical cues into intracellular activities, using a two-level affinity pull-down (phosphotyrosine antibody and titanium dioxide beads) method and mass spectrometry. This analysis identified ~1,000 tyrosine-phosphorylated proteins of TM cell-ECM adhesion complexes. Many consensus adhesome proteins were found to be tyrosine phosphorylated. Interestingly, several of the phosphotyrosinylated proteins found in TM cell-ECM adhesion complexes are known to be required for podocyte glomerular filtration, indicating the existence of molecular parallels that are likely relevant to the shared fluid barrier and filtration functions of the two mechanosensitive cell types.

Full Text

Duke Authors

Cited Authors

  • Maddala, R; Rao, PV

Published Date

  • August 1, 2020

Published In

Volume / Issue

  • 319 / 2

Start / End Page

  • C288 - C299

PubMed ID

  • 32432933

Pubmed Central ID

  • PMC7500213

Electronic International Standard Serial Number (EISSN)

  • 1522-1563

Digital Object Identifier (DOI)

  • 10.1152/ajpcell.00537.2019


  • eng

Conference Location

  • United States