The non-receptor tyrosine phosphatase type 14 blocks caveolin-1-enhanced cancer cell metastasis.

Oncogene
Natalia I Díaz-ValdiviaAndrew F G Quest

Abstract

Caveolin-1 (CAV1) enhanced migration, invasion, and metastasis of cancer cells is inhibited by co-expression of the glycoprotein E-cadherin. Although the two proteins form a multiprotein complex that includes β-catenin, it remained unclear how this would contribute to blocking the metastasis promoting function of CAV1. Here, we characterized by mass spectrometry the protein composition of CAV1 immunoprecipitates from B16F10 murine melanoma cells expressing or not E-cadherin. The novel protein tyrosine phosphatase PTPN14 was identified by mass spectrometry analysis exclusively in co-immunoprecipitates of CAV1 with E-cadherin. Interestingly, PTPN14 is implicated in controlling metastasis, but only few known PTPN14 substrates exist. We corroborated by western blotting experiments that PTPN14 and CAV1 co-inmunoprecipitated in the presence of E-cadherin in B16F10 melanoma and other cancer cells. Moreover, the CAV1(Y14F) mutant protein was shown to co-immunoprecipitate with PTPN14 even in the absence of E-cadherin, and overexpression of PTPN14 reduced CAV1 phosphorylation on tyrosine-14, as well as suppressed CAV1-enhanced cell migration, invasion and Rac-1 activation in B16F10, metastatic colon [HT29(US)] and breast cancer (MDA-MB-2...Continue Reading

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Citations

May 23, 2020·Cancer Metastasis Reviews·Timothy H WongIvan R Nabi
Oct 23, 2020·The Journal of Membrane Biology·Natasha BuwaNagaraj Balasubramanian
Mar 13, 2021·The Biochemical Journal·Katherine A YoungHayley J Sharpe

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Methods Mentioned

BETA
GTPases
GTPase
pull-down
co-immunoprecipitation
protein assay
immunoprecipitation

Software Mentioned

INSTAT
GraphPad
Mascot Proteome Discoverer
Mascot
ImageJ

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