Regulation of gelsolin to plant actin filaments and its distribution in pollen

被引:0
|
作者
陶志华
任海云
机构
[1] , Beijing100875, China
[2] Institute of Cell Biology, Collegeof Life Science, Beijing Normal University,Institute of Cell Biology, Collegeof Life Science, Beijing Normal University Beijing100875, China
[3] State Key Laboratory of Plant Physiologyand Biochemistry, Beijing100094,China
关键词
plant actin; gelsolin; pollen;
D O I
暂无
中图分类号
Q946 [植物生物化学];
学科分类号
摘要
The effect of plasma gelsolin on plant microfilaments and its localization in plant cells were investigated. The results by using ultracentrifugation and electron microscopy showed that plant microfilaments could be severed into shorter fragments by gelsolin in a Ca2+-dependent manner. By measuring the binding ability of plasma gelsolin to pollen actin using the method of immunoprecipitation, it was shown that pollen actin could bind gelsolin at a ratio of 2.0±0.21 in the presence of Ca2+. Addition of EGTA could disassociate the actin-gelsolin complexes, reducing the ratio to 1.2±0.23, and the addition of PIP2 could further reduce the ratio to 0.8±0.1. The results indicate that plant actin has similar binding properties with plasma gelsolin as that of animal actin. By Western blotting we identified the existence of gelsolin in lily pollen. The results of immunolo- calization of gelsolin in pollen and pollen tube showed that gelsolin was mainly localized at the germinal furrow in pollen grains and at the cytoplasm in pollen tube, especially in the tip region.
引用
收藏
页码:379 / 388
页数:10
相关论文
共 50 条
  • [31] Molecular dynamics study of interactions between polymorphic actin filaments and gelsolin segment-1
    Lee, Myeongsang
    Kang, Ellen H.
    PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, 2020, 88 (02) : 385 - 392
  • [32] IDENTIFICATION OF A POLYPHOSPHOINOSITIDE-MODULATED DOMAIN IN GELSOLIN WHICH BINDS TO THE SIDES OF ACTIN-FILAMENTS
    YIN, HL
    IIDA, K
    JANMEY, PA
    JOURNAL OF CELL BIOLOGY, 1988, 106 (03): : 805 - 812
  • [33] Structure, regulation and related diseases of the actin-binding protein gelsolin
    Feldt, Jessica
    Schicht, Martin
    Garreis, Fabian
    Welss, Jessica
    Schneider, Ulrich W.
    Paulsen, Friedrich
    EXPERT REVIEWS IN MOLECULAR MEDICINE, 2018, 20
  • [34] Activation of cytosolic Slingshot-1 phosphatase by gelsolin-generated soluble actin filaments
    Takahashi, Katsunori
    Kanno, Shin-ichiro
    Mizuno, Kensaku
    BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2014, 454 (03) : 471 - 477
  • [35] Structure, regulation and related diseases of the actin-binding protein gelsolin
    Feldt, Jessica
    Schicht, Martin
    Garreis, Fabian
    Welss, Jessica
    Schneider, Ulrich W.
    Paulsen, Friedrich
    EXPERT REVIEWS IN MOLECULAR MEDICINE, 2019, 20
  • [36] EVIDENCE FOR AN ATP CAP AT THE ENDS OF ACTIN-FILAMENTS AND ITS REGULATION OF THE F-ACTIN STEADY-STATE
    CARLIER, MF
    PANTALONI, D
    KORN, ED
    JOURNAL OF BIOLOGICAL CHEMISTRY, 1984, 259 (16) : 9983 - 9986
  • [37] Organization and regulation of the actin cytoskeleton in the pollen tube
    Qu, Xiaolu
    Jiang, Yuxiang
    Chang, Ming
    Liu, Xiaonan
    Zhang, Ruihui
    Huang, Shanjin
    FRONTIERS IN PLANT SCIENCE, 2015, 5
  • [38] DISTRIBUTION OF ACTIN, MYOSIN, ACTIN-BINDING PROTEIN AND GELSOLIN IN CULTURED LYMPHOID-CELLS
    THORSTENSSON, R
    UTTER, G
    NORBERG, R
    FAGRAEUS, A
    HARTWIG, JH
    YIN, HL
    STOSSEL, TP
    EXPERIMENTAL CELL RESEARCH, 1982, 140 (02) : 395 - 400
  • [39] Regulation of epithelial sodium channels by short actin filaments
    Berdiev, BK
    Prat, AG
    Cantiello, HF
    Ausiello, DA
    Fuller, CM
    Jovov, B
    Benos, DJ
    Ismailov, II
    JOURNAL OF BIOLOGICAL CHEMISTRY, 1996, 271 (30) : 17704 - 17710
  • [40] Remodeling of Actin Filaments by Drebrin A and Its Implications
    Grintsevich, Elena E.
    DREBRIN: FROM STRUCTURE AND FUNCTION TO PHYSIOLOGICAL AND PATHOLOGICAL ROLES, 2017, 1006 : 61 - 82