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Cancer and Metastasis Reviews

, Volume 35, Issue 2, pp 179–199 | Cite as

Understanding the cellular roles of Fyn-related kinase (FRK): implications in cancer biology

  • Raghuveera Kumar Goel
  • Kiven Erique LukongEmail author
NON-THEMATIC REVIEW

Abstract

The non-receptor tyrosine kinase Fyn-related kinase (FRK) is a member of the BRK family kinases (BFKs) and is distantly related to the Src family kinases (SFKs). FRK was first discovered in 1993, and studies pursued thereafter attributed a potential tumour-suppressive function to the enzyme. In recent years, however, further functional characterization of the tyrosine kinase in diverse cancer types suggests that FRK may potentially play an oncogenic role as well. Specifically, while ectopic expression of FRK suppresses cell proliferation and migration in breast and brain cancers, knockdown or catalytic inhibition of FRK suppresses these cellular processes in pancreatic and liver cancer. Such functional paradox is therefore evidently exhibited in a tissue-specific context. This review sheds light on the recent developments emerged from investigations on FRK which include: (a) a review of the expression pattern of the protein in mammalian cells/tissues, (b) underlying genomic perturbations and (c) a mechanistic function of the enzyme across different cellular environments. Given its functional heterogeneity observed across different cancers, we also discuss the therapeutic significance of FRK.

Keywords

FRK Rak PTK5 SRMS BRK Src Breast cancer Tyrosine kinase Tumour suppressor Oncogene BFKs Fyn PTEN 

Notes

Acknowledgments

The authors apologize to those whose work was not included owing to space limitations. Breast cancer research in the Lukong lab is supported over the years by funds from various organizations including the Canadian Breast Cancer Foundation (CBCF) and Canadian Institutes of Health Research (CIHR).

Compliance with ethical standards

Conflict of interest

The authors are unaware of any affiliations, memberships, or financial holdings that might be perceived as affecting the objectivity of this review.

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Copyright information

© Springer Science+Business Media New York 2016

Authors and Affiliations

  1. 1.Department of BiochemistryUniversity of SaskatchewanSaskatoonCanada

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