The phosphatase Shp1 interacts with and dephosphorylates cortactin to inhibit invadopodia function.

ABSTRACT:

Background

Invadopodia are actin-based cell-membrane protrusions associated with the extracellular matrix degradation accompanying cancer invasion. The elucidation of the molecular mechanisms leading to invadopodia formation and activity is central for the prevention of tumor spreading and growth. Protein tyrosine kinases such as Src are known to regulate invadopodia assembly, little is however known on the role of protein tyrosine phosphatases in this process. Among these enzymes, we have selected the tyrosine phosphatase Shp1 to investigate its potential role in invadopodia assembly, due to its involvement in cancer development.

Methods

Co-immunoprecipitation and immunofluorescence studies were employed to identify novel substrate/s of Shp1AQ controlling invadopodia activi

SUBMITTER: Varone A 

PROVIDER: S-EPMC8176763 | biostudies-literature | 2021 Jun

REPOSITORIES: biostudies-literature