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Journal of Hematology and Oncology

, 8:47

First Online: 09 May 2015Received: 16 February 2015Accepted: 27 April 2015DOI: 10.1186-s13045-015-0144-2

Cite this article as: Liu, S., Xiong, X., Zhao, X. et al. J Hematol Oncol 2015 8: 47. doi:10.1186-s13045-015-0144-2

Abstract

Eukaryotic cell membrane dynamics change in curvature during physiological and pathological processes. In the past ten years, a novel protein family, Fes-CIP4 homology-Bin-Amphiphysin-Rvs F-BAR domain proteins, has been identified to be the most important coordinators in membrane curvature regulation. The F-BAR domain family is a member of the Bin-Amphiphysin-Rvs BAR domain superfamily that is associated with dynamic changes in cell membrane. However, the molecular basis in membrane structure regulation and the biological functions of F-BAR protein are unclear. The pathophysiological role of F-BAR protein is unknown. This review summarizes the current understanding of structure and function in the BAR domain superfamily, classifies F-BAR family proteins into nine subfamilies based on domain structure, and characterizes F-BAR protein structure, domain interaction, and functional relevance. In general, F-BAR protein binds to cell membrane via F-BAR domain association with membrane phospholipids and initiates membrane curvature and scission via Src homology-3 SH3 domain interaction with its partner proteins. This process causes membrane dynamic changes and leads to seven important cellular biological functions, which include endocytosis, phagocytosis, filopodium, lamellipodium, cytokinesis, adhesion, and podosome formation, via distinct signaling pathways determined by specific domain-binding partners. These cellular functions play important roles in many physiological and pathophysiological processes. We further summarize F-BAR protein expression and mutation changes observed in various diseases and developmental disorders. Considering the structure feature and functional implication of F-BAR proteins, we anticipate that F-BAR proteins modulate physiological and pathophysiological processes via transferring extracellular materials, regulating cell trafficking and mobility, presenting antigens, mediating extracellular matrix degradation, and transmitting signaling for cell proliferation.

KeywordsF-BAR proteins Membrane dynamics Cellular functions Pathophysiology AbbreviationsArp2-3Actin-related protein 2-3

BARBin-Amphiphysin-Rvs

CIP4CDC42-interacting protein 4

CRIBCDC42-Rac interactive binding

ECMExtracellular matrix

F-actinFilamentous actin

F-BARFes-CIP4 homology-Bin-Amphiphysin-Rvs

FCHOFCH only

FCHSDFCH and double SH3 domain proteins

FERFES related

FXF-BAR extension

GAS7Growth arrest-specific 7

HR1Protein kinase C-related kinase homology region 1

I-BARInverse BAR

N-BARN-terminal amphipathic helix BAR

NOSTRINNitric oxide synthase traffic inducer

N-WASPNeural Wiskott-Aldrich syndrome protein

PACSINProtein kinase C and casein kinase 2 substrates in neurons

RhoGAPRho GTPase-activating protein

SH2Src homology-2

SH3Src homology-3

srGAPSlit-Robo GTPase-activating protein

μHDμ-homology domain

VCAVerprolin, cofilin, acidic

WASPWiskott-Aldrich syndrome protein

WAVEWASP family verproline-homologous protein

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Autor: Suxuan Liu - Xinyu Xiong - Xianxian Zhao - Xiaofeng Yang - Hong Wang

Fuente: https://link.springer.com/







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