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

doi:10.1016/j.bbamcr.2015.11.002

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

University of Amsterdam

Research output: Contribution to journal › Review article › Academic › peer-review

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. (C) 2015 Elsevier B.V. All rights reserved

Original language	English
Pages (from-to)	219-228
Number of pages	10
Journal	BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH
Volume	1863
Issue number	2
DOIs	https://doi.org/10.1016/j.bbamcr.2015.11.002
Publication status	Published - 1 Feb 2016

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

Keywords

Cardiovascular function
LIM-only protein FHL2
Protein-protein interactions
Signaling pathways

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10.1016/j.bbamcr.2015.11.002

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title = "Protein-protein interactions of the LIM-only protein FHL2 and functional implication of the interactions relevant in cardiovascular disease",

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. (C) 2015 Elsevier B.V. All rights reserved",

keywords = "Cardiovascular function, LIM-only protein FHL2, Protein-protein interactions, Signaling pathways",

author = "Tran, \{M. Khang\} and Kondababu Kurakula and Koenis, \{Duco S.\} and \{de Vries\}, \{Carlie J. M.\}",

note = "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: {\textcopyright} 2015 Elsevier B.V.",

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doi = "10.1016/j.bbamcr.2015.11.002",

language = "English",

volume = "1863",

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journal = "BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH",

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}

Protein-protein interactions of the LIM-only protein FHL2 and functional implication of the interactions relevant in cardiovascular disease. / Tran, M. Khang; Kurakula, Kondababu; Koenis, Duco S. et al.
In: BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH, Vol. 1863, No. 2, 01.02.2016, p. 219-228.

Research output: Contribution to journal › Review article › Academic › peer-review

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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. (C) 2015 Elsevier B.V. All rights reserved

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. (C) 2015 Elsevier B.V. All rights reserved

KW - Cardiovascular function

KW - LIM-only protein FHL2

KW - Protein-protein interactions

KW - Signaling pathways

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U2 - 10.1016/j.bbamcr.2015.11.002

DO - 10.1016/j.bbamcr.2015.11.002

M3 - Review article

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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 -

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

Abstract

UN SDGs

Keywords

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