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Biochemical characteristics,functions and clinical significance of cofilin
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作者 Yi-Kang Yu Tian-Hang Chen +4 位作者 Zheng Liu Dong-Peng Tu Yi Peng Bin Zhang Chao Xu 《Life Research》 2021年第3期20-38,共19页
Cofilin is a low molecular weight actin-binding protein widely found in eukaryotic cells in ADF/cofilin family proteins,which has a wide range of biological effects and has gradually become a research hotspot in recen... Cofilin is a low molecular weight actin-binding protein widely found in eukaryotic cells in ADF/cofilin family proteins,which has a wide range of biological effects and has gradually become a research hotspot in recent years.We review the structural characteristics of cofilin,the mechanism of regulating actin,biological functions,and the relationship with clinical diseases to explore its role in the development of cancer,nervous system diseases,osteoarthritis,heart and kidney diseases.The use of cofilin phosphorylation pathways as major action-targeting sites in the treatment of these diseases could provide a basis for the development of new drugs,such as Rho related protein kinases inhibitors netarsudil to prevent cancer metastasis,neuroligin C-terminal domain(NLG1-CTD)peptides with high affinity to inhibit LIM kinase thereby preventing nervous system diseases,grape seed proanthocyanidins to inhibit cofilin related oxidative stress in the treatment of heart and kidney diseases. 展开更多
关键词 ADF/cofilin family protein actin binding protein actin regulation Clinical significance
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Plastins regulate ectoplasmic specialization via its actin bundling activity on microfilaments in the rat testis 被引量:3
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作者 Nan Li Chris KC Wong C Yan Cheng 《Asian Journal of Andrology》 SCIE CAS CSCD 2016年第5期716-722,共7页
Plastins are a family of actin binding proteins (ABPs) known to cross-link actin microfilaments in mammalian cells, creating actin microfilament bundles necessary to confer cell polarity and cell shape. Plastins als... Plastins are a family of actin binding proteins (ABPs) known to cross-link actin microfilaments in mammalian cells, creating actin microfilament bundles necessary to confer cell polarity and cell shape. Plastins also support cell movement in response to changes in environment, involved in cell/tissue growth and development. They also confer plasticity to cells and tissues in response to infection or other pathological conditions (e.g., inflammation). In the testis, the cell-cell anchoring junction unique to the testis that is found at the Sertoli cell-cell interface at the blood-testis barrier (BTB) and at the Sertoli-spermatid (e.g., 8-19 spermatids in the rat testis) is the basal and the apical ectoplasmic specialization (ES), respectively. The ES is an F-actin-rich anchoring junction constituted most notably by actin microfilament bundles. A recent report using RNAi that specifically knocks down plastin 3 has yielded some insightful information regarding the mechanism by which plastin 3 regulates the status of actin microfilament bundles at the ES via its intrinsic actin filament bundling activity. Herein, we provide a brief review on the role of plastins in the testis in light of this report, which together with recent findings in the field, we propose a likely model by which plastins regulate ES function during the epithelial cycle of sDermatogenesis via their intrinsic activity on actin microfilament organization in the rat testis. 展开更多
关键词 actin binding proteins actin bundling proteins CYTOSKELETON F-actin fimbrins plastins seminiferous epithelial cycle SPERMATOGENESIS TESTIS
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AtFH8 Is Involved in Root Development under Effect of Low-Dose Latrunculin B in Dividing Cells 被引量:7
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作者 Xiu-Hua Xue Chun-Qing Guo +3 位作者 Fei Du Quan-Long Lu Chuan-Mao Zhang Hai-Yun Ren 《Molecular Plant》 SCIE CAS CSCD 2011年第2期264-278,共15页
Formins have been paid much attention for their potent nucleating activity. However, the connection between the in vivo functions of AtFHs (Arabidopsis thaliana formin homologs) and their effects on actin organizati... Formins have been paid much attention for their potent nucleating activity. However, the connection between the in vivo functions of AtFHs (Arabidopsis thaliana formin homologs) and their effects on actin organization is poorly understood, in this study, we characterized the bundling activity of AtFH8 in vitro and in vivo. Biochemical analysis showed that AtFH8(FH1FH2) could form dimers and bundle preformed actin filaments or induce stellar structures during actin polymerization. Expression of truncated forms of AtFH8 and immunolocalization analysis showed that AtFH8 localized primarily to nuclear envelope in interphase and to the new cell wall after cytokinesis, depending primarily on its N-terminal transmembrane domain. GUS histochemical staining showed AtFH8 was predominantly expressed in Arabidopsis root meristem, vasculature, and outgrowth points of lateral roots. The primary root growth and lateral root initiation of atfh8 could be decreased by latrunculin B (LatB). Analysis of the number of dividing cells in Arabidopsis root tips showed that much fewer dividing cells in Lat B-treated atfh8 plants than wild-type plants, which indicates that AtFH8 was involved in cell division. Actin cytoskeleton in root meristem of atfh8-1 was more sensitive to LatB treatment than that of wild-type. Altogether, our results indicate that AtFH8 is an actin filament nucleator and bundler that functions in cell division and root development. 展开更多
关键词 actin binding protein FORMIN cell division root meristem lateral root initiation actin nucleator and bundler.
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