The structural features of Trask that mediate its anti-adhesive functions.

PLoS One

Department of Medicine, University of California San Francisco, San Francisco, California, United States of America.

Published: April 2011

AI Article Synopsis

  • Trask/CDCP1 is a transmembrane protein with two main parts: a large extracellular domain (ECD) and a small intracellular domain (ICD), where the ICD gets phosphorylated by Src kinases during loss of cell attachment, leading to decreased cell adhesion.
  • Proteolytic cleavage of the ECD by serine proteases occurs, but its significance is unclear; it does not seem to trigger the phosphorylation of the ICD.
  • Studies with deletion mutants show that the anti-adhesive function of Trask relies solely on the ICD's tyrosine phosphorylation, while the ECD does not influence this process, leaving the specific role of the ECD in cell adhesion functions still unknown.

Article Abstract

Trask/CDCP1 is a transmembrane protein with a large extracellular and small intracellular domains. The intracellular domain (ICD) undergoes tyrosine phosphorylation by Src kinases during anchorage loss and, when phosphorylated, Trask functions to inhibit cell adhesion. The extracellular domain (ECD) undergoes proteolytic cleavage by serine proteases, although the functional significance of this remains unknown. There is conflicting evidence regarding whether it functions to signal the phosphorylation of the ICD. To better define the structural determinants that mediate the anti-adhesive functions of Trask, we generated a series of deletion mutants of Trask and expressed them in tet-inducible cell models to define the structural elements involved in cell adhesion signaling. We find that the ECD is dispensable for the phosphorylation of the ICD or for the inhibition of cell adhesion. The anti-adhesive functions of Trask are entirely embodied within its ICD and are specifically due to tyrosine phosphorylation of the ICD as this function is completely lost in a phosphorylation-defective tyrosine-phenylalanine mutant. Both full length and cleaved ECDs are fully capable of phosphorylation and undergo phosphorylation during anchorage loss and cleavage is not an upstream signal for ICD phosphorylation. These data establish that the anti-adhesive functions of Trask are mediated entirely through its tyrosine phosphorylation. It remains to be defined what role, if any, the Trask ECD plays in its adhesion functions.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3084758PMC
http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0019154PLOS

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