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FNBP1 was involved with the morphological control in the hepatocyte
Author(s) -
Zhang Jun,
LIN Mingming,
Zhang Qianqing,
Wang Yunhong,
Zhu Chongyang,
Li Xin
Publication year - 2011
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.25.1_supplement.lb111
Subject(s) - microbiology and biotechnology , cytoskeleton , actin , endocytosis , cytochalasin d , actin cytoskeleton , biology , cell cortex , cell , biochemistry
The formin‐binding protein 1 (FNBP1) was widely expressed in eukaryotic cells with active participations in endocytosis and movement by simultaneously promoting tubular membrane invagination (or deformation) and actin cytoskeleton rearrangement. The N‐terminal EFC (extended FER‐CIP4 homology) domain of FNBP1 was previously shown to have membrane binding and deformation activities and capable of activating the WASP‐Arp2/3‐actin pathway. In the present investigation, it was curiously found that knockdown of the endogenous FNBP1 by RNA interference (RNAi) didn't affect endocytosis and movement in hepatocyte 7703 cells, but triggered the cell morphological remodeling from epithelioid to fibrous shape and actin specific reagents, either phalloidine or cytochalasin B, could abrogate the silence effect. Furthermore, withdrawal of the silence could induce the cell morphological recovery, which strongly suggested that FNBP1 also played a role in morphological control. The experiments, along with the published evidences, indicated that FNBP1 probably exerted various functions in different cellular contexts by sharing a common molecular process associated with actin cytoskeleton reorganization in cortex. This work was supported by a grant from National Natural Science Foundation of China (NSFC, no. 20803098)