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Title 

Identification of proteins suppressing the functions of oncogenic phosphatase of regenerating liver 1 and 3

Authors 

J D LeeHaiyoung JungS H Min

Publisher 

Korean Society of Medical Biochemistry

Issue Date 

2016

Citation 

Experimental and Therapeutic Medicine, vol. 12, no. 5, pp. 2974-2982

Keywords 

EMDFKBP8GBP1LRP10NDUFB8Phosphatase of regenerating liver 1Phosphatase of regenerating liver 3PLIN3RABAC1ScreeningSDC4SELPLGSYNE2TMUB2TPD52L2Yeast two-hybrid

Abstract 

The phosphatase of regenerating liver (PRL) family, including PRL-1, PRL-2, and PRL-3, comprises protein tyrosine phosphatases whose deregulation is associated with the tumorigenesis and metastasis of many types of cancer. However, the underlying mechanism is poorly understood. In this study, aiming to increase understanding of the molecular mechanisms underlying the functions of PRL-1 and PRL-3, a yeast two-hybrid system was employed to screen for their interacting proteins. Alignment with the NCBI BLAST database revealed 12 interactive proteins: Synaptic nuclear envelope protein 2, emerin, mannose 6-phosphate receptor-binding protein 1, low-density lipoprotein receptor-related protein 10, Rab acceptor 1, tumor protein D52-like 2, selectin P ligand (SELPLG), guanylate binding protein 1, transmembrane and ubiquitin-like domain-containing 2, NADH:ubiquinone oxido-reductase subunit B8, syndecan 4 and FK506-binding protein 8 (FKBP8). These proteins are associated with cell proliferation, apoptosis, immune response, cell fate specification and metabolic process in biological process categories, and involved in various signaling pathways, including Alzheimer's disease, Parkinson's disease, Huntington's disease, hypertrophic cardio-myopathy and cell adhesion molecules. Interactions of PRL-1 with the prey proteins SELPLG and FKBP8 were confirmed by immunoprecipitation or immunostaining. Furthermore, SELPLG and FKBP8 suppressed PRL-1- or PRL-3-mediated p53 activity. Identification of the proteins interacting with PRL family proteins may provide valuable information to better understand the mechanism of PRL-mediated signal transduction in cancer and other diverse diseases.

ISSN 

1792-0981

Link 

http://dx.doi.org/10.3892/etm.2016.3722

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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