The role of dynamin in the assembly and function of podosomes and invadopodia

被引:81
作者
McNiven, MA
Baldassarre, M
Buccione, R [1 ]
机构
[1] Consorzio Mario Negri Sud, Dept Cell Biol & Oncol, I-66030 Chieti, Italy
[2] Mayo Clin & Mayo Fdn, Dept Biochem & Mol Biol, Ctr Basic Res Digest Dis, Rochester, MN 55905 USA
来源
FRONTIERS IN BIOSCIENCE-LANDMARK | 2004年 / 9卷
关键词
dynamin; podosomes; invadopodia; cell invasion; review;
D O I
10.2741/1348
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Cells make contact with the extracellular matrix (ECM) through extensions of the plasma membrane; these range from irregular dynamic structures, e. g. lamellipodia, ruffles and pseudopodia, to more localized and highly defined protrusions, e. g. podosomes and invadopodia. Both might be instruments through which cells sample the immediate extracellular environment and maintain polarized activities such as chemotaxis and focal degradation of the matrix. Podosomes are expressed in cells of the monocytic lineage, and most studies point to a role for podosomes in adhesion/motility. Invadopodia are prominent in certain aggressive cancer cells (or transformed cells) and appear to be directly responsible for focal ECM degradation. Recent studies have revived interest in these structures in terms of the actin regulation machinery. Within this framework, the atypical GTP-binding protein dynamin, a central modulator of protrusive events, has been associated to podosome and invadopodia structure and function. Here, we specifically discuss the role played by dynamin in controlling the activities and function of these structures.
引用
收藏
页码:1944 / 1953
页数:10
相关论文
共 85 条
  • [1] Adams JC, 2002, J CELL SCI, V115, P257
  • [2] Cell-matrix contact structures
    Adams, JC
    [J]. CELLULAR AND MOLECULAR LIFE SCIENCES, 2001, 58 (03) : 371 - 392
  • [3] Dynamin participates in focal extracellular matrix degradation by invasive cells
    Baldassarre, M
    Pompeo, A
    Beznoussenko, G
    Castaldi, C
    Cortellino, S
    McNiven, MA
    Luini, A
    Buccione, R
    [J]. MOLECULAR BIOLOGY OF THE CELL, 2003, 14 (03) : 1074 - 1084
  • [4] Focalized proteolysis: Spatial and temporal regulation of extracellular matrix degradation at the cell surface
    Basbaum, CB
    Werb, Z
    [J]. CURRENT OPINION IN CELL BIOLOGY, 1996, 8 (05) : 731 - 738
  • [5] Phosphatidylinositol 4,5-biphosphate (PIP2)-induced vesicle movement depends on N-WASP and involves Nck, WIP, and Grb2
    Benesch, S
    Lommel, S
    Steffen, A
    Stradal, TEB
    Scaplehorn, N
    Way, M
    Wehland, J
    Rottner, K
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (40) : 37771 - 37776
  • [6] An invasion-related complex of cortactin, paxillin and PKCμ associates with invadopodia at sites of extracellular matrix degradation
    Bowden, ET
    Barth, M
    Thomas, D
    Glazer, RI
    Mueller, SC
    [J]. ONCOGENE, 1999, 18 (31) : 4440 - 4449
  • [7] Bowden ET, 2001, METHOD CELL BIOL, V63, P613
  • [8] Regulation of Wiskott-Aldrich syndrome protein and related molecules
    Caron, E
    [J]. CURRENT OPINION IN CELL BIOLOGY, 2002, 14 (01) : 82 - 87
  • [9] Specialized surface protrusions of invasive cells, invadopodia and lamellipodia, have differential MT1-MMP, MMP-2, and TIMP-2 localization
    Chen, WT
    Wang, JY
    [J]. INHIBITION OF MATRIX METALLOPROTEINASES: THERAPEUTIC APPLICATIONS, 1999, 878 : 361 - 371
  • [10] Proteases associated with invadopodia, and their role in degradation of extracellular matrix
    Chen, WT
    [J]. ENZYME & PROTEIN, 1996, 49 (1-3) : 59 - 71