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01-12-2017 | NON-THEMATIC REVIEW

Myristoylated alanine-rich C kinase substrate (MARCKS): a multirole signaling protein in cancers

Authors: Lon Wolf R. Fong, David C. Yang, Ching-Hsien Chen

Published in: Cancer and Metastasis Reviews | Issue 4/2017

Abstract

Emerging evidence implicates myristoylated alanine-rich C-kinase substrate (MARCKS), a major substrate of protein kinase C (PKC), in a critical role for cancer development and progression. MARCKS is tethered to the plasma membrane but can shuttle between the cytosol and plasma membrane via the myristoyl-electrostatic switch. Phosphorylation of MARCKS by PKC leads to its translocation from the plasma membrane to the cytosol where it functions in actin cytoskeletal remodeling, Ca²⁺ signaling through binding to calmodulin, and regulation of exocytic vesicle release in secretory cells such as neurons and airway goblet cells. Although the contribution of MARCKS to various cellular processes has been extensively studied, its roles in neoplastic disease have been conflicting. This review highlights the molecular and functional differences of MARCKS that exist between normal and tumor cells. We also discuss the recent advances in the potential roles of MARCKS in tumorigenesis, metastasis, and resistance to anti-cancer therapies, with a focus on addressing the inconsistent results regarding the function of MARCKS as a promoter or inhibitor of oncogenesis.

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Title: Myristoylated alanine-rich C kinase substrate (MARCKS): a multirole signaling protein in cancers
Authors: Lon Wolf R. Fong
David C. Yang
Ching-Hsien Chen
Publication date: 01-12-2017
Publisher: Springer US
Published in: Cancer and Metastasis Reviews / Issue 4/2017
Print ISSN: 0167-7659
Electronic ISSN: 1573-7233
DOI: https://doi.org/10.1007/s10555-017-9709-6

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