TY - JOUR
T1 - Protein-protein interactions of the LIM-only protein FHL2 and functional implication of the interactions relevant in cardiovascular disease
AU - Tran, M. Khang
AU - Kurakula, Kondababu
AU - Koenis, Duco S.
AU - de Vries, Carlie J.M.
N1 - Funding Information: This study is supported by project P1.02 NEXTREAM of the research program of the BioMedical Materials Institute, co-funded by the Dutch Ministry of Economic Affairs. The financial contribution of the Dutch Heart Foundation is gratefully acknowledged. We acknowledge the support from the Netherlands CardioVascular Research Initiative: “Dutch Heart Foundation, Dutch Federation of University Medical Centers, the Netherlands Organization for Health Research and Development and the Royal Netherlands Academy of Sciences” for the GENIUS project (CVON2011-19) and funding by the Rembrandt Institute Cardiovascular Sciences , the Netherlands ( RICS-2013-deVries/Versteeg ). Publisher Copyright: © 2015 Elsevier B.V.
PY - 2016/2/1
Y1 - 2016/2/1
N2 - 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.
AB - 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.
KW - Cardiovascular function
KW - LIM-only protein FHL2
KW - Protein-protein interactions
KW - Signaling pathways
UR - http://www.scopus.com/inward/record.url?scp=84947996590&partnerID=8YFLogxK
U2 - https://doi.org/10.1016/j.bbamcr.2015.11.002
DO - https://doi.org/10.1016/j.bbamcr.2015.11.002
M3 - Review article
C2 - 26548523
SN - 0167-4889
VL - 1863
SP - 219
EP - 228
JO - Biochimica et Biophysica Acta - Molecular Cell Research
JF - Biochimica et Biophysica Acta - Molecular Cell Research
IS - 2
ER -