Structure and functions of His domain protein tyrosine phosphatase in receptor trafficking and cancer

Author:

Desrochers Guillaume12,Kazan Jalal M.12,Pause Arnim12

Affiliation:

1. Department of Biochemistry, McGill University, Montréal, QC H3G 1Y6, Canada.

2. Goodman Cancer Research Centre, McGill University, Montréal, QC H3A 1A3, Canada.

Abstract

Cell surface receptors trigger the activation of signaling pathways to regulate key cellular processes, including cell survival and proliferation. Internalization, sorting, and trafficking of activated receptors, therefore, play a major role in the regulation and attenuation of cell signaling. Efficient sorting of endocytosed receptors is performed by the ESCRT machinery, which targets receptors for degradation by the sequential establishment of protein complexes. These events are tightly regulated and malfunction of ESCRT components can lead to abnormal trafficking and sustained signaling and promote tumor formation or progression. In this review, we analyze the modular domain organization of the alternative ESCRT protein HD-PTP and its role in receptor trafficking and tumorigenesis.

Publisher

Canadian Science Publishing

Subject

Cell Biology,Molecular Biology,Biochemistry

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