PONTICULIN IS THE MAJOR HIGH-AFFINITY LINK BETWEEN THE PLASMA-MEMBRANE AND THE CORTICAL ACTIN NETWORK IN DICTYOSTELIUM

被引:45
作者
HITT, AL [1 ]
HARTWIG, JH [1 ]
LUNA, EJ [1 ]
机构
[1] BRIGHAM & WOMENS HOSP,DEPT EXPTL MED,BOSTON,MA 02115
关键词
D O I
10.1083/jcb.126.6.1433
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Interactions between the plasma membrane and underlying actin-based cortex have been implicated in membrane organization and stability, the control of cell shape, and various motile processes. To ascertain the function of high affinity actin-membrane associations, we have disrupted by homologous recombination the gene encoding ponticulin, the major high affinity actin-membrane link in Dictyostelium discoideum amoebae. Cells lacking detectable amounts of ponticulin message and protein also are deficient in high affinity actin-membrane binding by several criteria. First, only 10-13% as much endogenous actin cosediments through sucrose and crude plasma membranes from ponticulin-minus cells, as compared with membranes from the parental strain. Second, purified plasma membranes exhibit little or no binding or nucleation of exogenous actin in vitro. Finally only 10-30% as much endogenous actin partitions with plasma membranes from ponticulin-minus cells after these cells are mechanically unroofed with polylysine-coated coverslips. The loss of the cell's major actin-binding membrane protein appears to be surprisingly benign under laboratory conditions. Ponticulin-minus cells grow normally in axenic culture and pinocytose FITC-dextran at the same rate as do parental cells. The rate of phagocytosis of particles by ponticulin-minus cells in growth media also is unaffected. By contrast, after initiation of development, cells lacking ponticulin aggregate faster than the parental cells. Subsequent morphogenesis proceeds asynchronously, but viable spores can form. These results indicate that ponticulin is not required for cellular translocation, but apparently plays a role in cell patterning during development.
引用
收藏
页码:1433 / 1444
页数:12
相关论文
共 70 条
[61]  
TAYLOR DL, 1973, J CELL BIOL, V59, P378, DOI 10.1083/jcb.59.2.378
[62]   THE UNCONVENTIONAL MYOSIN ENCODED BY THE MYOA GENE PLAYS A ROLE IN DICTYOSTELIUM MOTILITY [J].
TITUS, MA ;
WESSELS, D ;
SPUDICH, JA ;
SOLL, D .
MOLECULAR BIOLOGY OF THE CELL, 1993, 4 (02) :233-246
[63]  
VANHAASTERT PJM, 1991, EUR J BIOCHEM, V195, P289
[64]  
VOGEL G, 1987, METHOD CELL BIOL, V28, P129
[65]   THE YEAST ACTIN CYTOSKELETON [J].
WELCH, MD ;
HOLTZMAN, DA ;
DRUBIN, DG .
CURRENT OPINION IN CELL BIOLOGY, 1994, 6 (01) :110-119
[66]   MYOSIN IB NULL MUTANTS OF DICTYOSTELIUM EXHIBIT ABNORMALITIES IN MOTILITY [J].
WESSELS, D ;
MURRAY, J ;
JUNG, G ;
HAMMER, JA ;
SOLL, DR .
CELL MOTILITY AND THE CYTOSKELETON, 1991, 20 (04) :301-315
[67]   HOMOLOGOUS RECOMBINATION IN THE DICTYOSTELIUM ALPHA-ACTININ GENE LEADS TO AN ALTERED MESSENGER-RNA AND LACK OF THE PROTEIN [J].
WITKE, W ;
NELLEN, W ;
NOEGEL, A .
EMBO JOURNAL, 1987, 6 (13) :4143-4148
[68]   REDUNDANCY IN THE MICROFILAMENT SYSTEM - ABNORMAL-DEVELOPMENT OF DICTYOSTELIUM CELLS LACKING 2 F-ACTIN CROSS-LINKING PROTEINS [J].
WITKE, W ;
SCHLEICHER, M ;
NOEGEL, AA .
CELL, 1992, 68 (01) :53-62
[69]   F-ACTIN BINDS TO THE CYTOPLASMIC SURFACE OF PONTICULIN, A 17-KD INTEGRAL GLYCOPROTEIN FROM DICTYOSTELIUM-DISCOIDEUM PLASMA-MEMBRANES [J].
WUESTEHUBE, LJ ;
LUNA, EJ .
JOURNAL OF CELL BIOLOGY, 1987, 105 (04) :1741-1751
[70]   RECENT QUANTITATIVE STUDIES OF ACTIN FILAMENT TURNOVER DURING CELL LOCOMOTION [J].
ZIGMOND, SH .
CELL MOTILITY AND THE CYTOSKELETON, 1993, 25 (04) :309-316