Protein-protein interactions of the LIM-only protein FHL2 and functional implication of the interactions relevant in cardiovascular disease.

M Khang Tran, Kondababu Kurakula, Duco S Koenis, Carlie J M de Vries

Journal: Biochimica et biophysica acta 2016;1863(2):219-28

PMID: 26548523

Free Full Text on Elsevier Science View on PubMed

Abstract

FHL2 belongs to the LIM-domain only proteins and contains four and a half LIM domains, each of which are composed of two zinc finger structures. FHL2 exhibits specific interaction with proteins exhibiting diverse functions, including transmembrane receptors, transcription factors and transcription co-regulators, enzymes, and structural proteins. The function of these proteins is regulated by FHL2, which modulates intracellular signal transduction pathways involved in a plethora of cellular tasks. The present review summarizes the current knowledge on the protein interactome of FHL2 and provides an overview of the functional implication of these interactions in apoptosis, migration, and regulation of nuclear receptor function. FHL2 was originally identified in the heart and there is extensive literature available on the role of FHL2 in the cardiovascular system, which is also summarized in this review.

Address: Department of Medical Biochemistry, Academic Medical Center, University of Amsterdam, Amsterdam, The Netherlands.; Department of Medical Biochemistry, Academic Medical Center, University of Amsterdam, Amsterdam, The Netherlands. Electronic address: [email protected].

DOI: 10.1016/j.bbamcr.2015.11.002

Link outs

Free resources

Full Text Sources:

https://linkinghub.elsevier.com/retrieve/pii/S0167...

Other Literature Sources:

https://scite.ai/reports/26548523

MeSH Terms: Cardiovascular Diseases, Cell Membrane, Cell Nucleus, Cytoplasm, Humans, LIM-Homeodomain Proteins, Models, Biological, Models, Molecular, Muscle Proteins, Protein Interaction Mapping, Protein Structure, Tertiary, Transcription Factors