Striatins and the STRIPAK complex partners in the clinical outcome of patients with breast cancer and responses to drug treatment

Li, Amber Xinyu, Martin, Tracey A. ORCID: https://orcid.org/0000-0003-2690-4908, Ye, Lin ORCID: https://orcid.org/0000-0002-0303-2409, Ruge, Fiona, Sanders, Andrew J. ORCID: https://orcid.org/0000-0002-7997-5286, Khan, Elyas, Dou, Q. Ping, Davies, Eleri and Jiang, Wen G. ORCID: https://orcid.org/0000-0002-3283-1111 2023. Striatins and the STRIPAK complex partners in the clinical outcome of patients with breast cancer and responses to drug treatment. Chinese Journal of Cancer Research 35 , pp. 365-385. 10.21147/j.issn.1000-9604.2023.04.04

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Abstract

The investigation on the striatins (STRNs) family arose from two decades ago when Muro et al. identified a protein, which is now known as striatin-3 (STRN3 or SG2NA), during the S and G2 phase of the cell cycle by using antibodies acquired from cancer patient (1). While this study was being conducted, another research, which speculated the activities of adenylyl cyclase at the synapses, had coincidently discovered a WD-repeat family protein, called STRN, highly expressed at the dendritic sites in rat brain (2). The final member constituting the STRNs family, zinedin, was discovered in 2000 and was renamed later as striatin-4 (STRN4) (3). The three STRNs are homologous proteins that contain similar number of amino acids and possess identical interacting domain structure including a caveolin-binding domain, a coiled-coil region, a calmodulin (CaM, or CALM1) binding domain and a WD-repeat domain. Consistent with the presence of those domains, STRNs appear to associate with caveolin-1 and calmodulin in a Ca2+ dependent manner (4,5). It is now established that the members within the STRNs family are both cytosolic and membrane-bound proteins, and recently STRNs have also been suggested to function as cell adhesion regulators at both adherens junctions and tight junctions in epithelial cells (3,6). Although the full functions of STRNs were not entirely clear, the findings that they interacted with protein phosphatases, namely protein phosphatase 2A (PP2A) (coded by the PPP2CA gene) and PP2B (protein phosphatase 2B) (coded by the PPP2CB gene) indicated their role in regulating the phosphatases and phosphorylation events.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Medicine
Publisher:	Chinese Anti-Cancer Association
ISSN:	1000-9604
Funders:	Cardiff University China Medical Scholarship
Date of First Compliant Deposit:	29 August 2023
Date of Acceptance:	15 August 2023
Last Modified:	14 Nov 2024 08:15
URI:	https://orca.cardiff.ac.uk/id/eprint/162071

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