Microtubule-Associated Serine/Threonine (MAST) Kinases in Development and Disease

Overview

Journal Int J Mol Sci

Publisher MDPI

Specialties Biochemistry
Chemistry
Molecular Biology

Date 2023 Aug 12

PMID 37569286

Authors

Marie Rumpf

Sabine Pautz

Benedikt Drebes

Friedrich W Herberg

Hans-Arno J Muller

Affiliations

Soon will be listed here.

Abstract

Microtubule-Associated Serine/Threonine (MAST) kinases represent an evolutionary conserved branch of the AGC protein kinase superfamily in the kinome. Since the discovery of the founding member, MAST2, in 1993, three additional family members have been identified in mammals and found to be broadly expressed across various tissues, including the brain, heart, lung, liver, intestine and kidney. The study of MAST kinases is highly relevant for unraveling the molecular basis of a wide range of different human diseases, including breast and liver cancer, myeloma, inflammatory bowel disease, cystic fibrosis and various neuronal disorders. Despite several reports on potential substrates and binding partners of MAST kinases, the molecular mechanisms that would explain their involvement in human diseases remain rather obscure. This review will summarize data on the structure, biochemistry and cell and molecular biology of MAST kinases in the context of biomedical research as well as organismal model systems in order to provide a current profile of this field.

Citing Articles

The MAST kinase KIN-4 carries out mitotic entry functions of Greatwall in C. elegans.

Roumbo L, Ossareh-Nazari B, Vigneron S, Stefani I, Van Hove L, Legros V EMBO J. 2025; .

PMID: 39962268 DOI: 10.1038/s44318-025-00364-w.

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