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Titolo:
Regulated interactions between dynamin and the actin-binding protein cortactin modulate cell shape
Autore:
McNiven, MA; Kim, L; Krueger, EW; Orth, JD; Cao, H; Wong, TW;
Indirizzi:
Mayo Clin & Mayo Fdn, Dept Biochem & Mol Biol, Rochester, MN 55905 USA Mayo Clin & Mayo Fdn Rochester MN USA 55905 Biol, Rochester, MN 55905 USA Mayo Clin & Mayo Fdn, Ctr Basic Res Digest Dis, Rochester, MN 55905 USA Mayo Clin & Mayo Fdn Rochester MN USA 55905 Dis, Rochester, MN 55905 USA Univ Med & Dent New Jersey, Robert Wood Johnson Med Sch, Dept Biochem, Piscataway, NJ 08854 USA Univ Med & Dent New Jersey Piscataway NJ USA 08854 scataway, NJ 08854 USA
Titolo Testata:
JOURNAL OF CELL BIOLOGY
fascicolo: 1, volume: 151, anno: 2000,
pagine: 187 - 198
SICI:
0021-9525(20001002)151:1<187:RIBDAT>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
CULTURED HIPPOCAMPAL-NEURONS; TYROSINE PHOSPHORYLATION; MAMMALIAN-CELLS; ANIMAL-CELLS; SUBSTRATE; IDENTIFICATION; DISTINCT; FAMILY; SRC;
Keywords:
dynamin; actin; cortactin; cell shape; lamellipodia;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
29
Recensione:
Indirizzi per estratti:
Indirizzo: McNiven, MA Mayo Clin & Mayo Fdn, Dept Biochem & Mol Biol, 1721 GuggenheimBldg, Rochester, MN 55905 USA Mayo Clin & Mayo Fdn 1721 Guggenheim Bldg Rochester MN USA 55905
Citazione:
M.A. McNiven et al., "Regulated interactions between dynamin and the actin-binding protein cortactin modulate cell shape", J CELL BIOL, 151(1), 2000, pp. 187-198

Abstract

The dynamin family of large GTPases has been implicated in the formation of nascent vesicles in both the endocytic and secretory pathways. It is believed that dynamin interacts with a variety of cellular proteins to constrict membranes. The actin cytoskeleton has also been implicated in altering membrane shape and form during cell migration, endocytosis, and secretion andhas been postulated to work synergistically with dynamin and coat proteinsin several of these important processes, We have observed that the cytoplasmic distribution of dynamin changes dramatically in fibroblasts that have been stimulated to undergo migration with a motagen/hormone, In quiescent cells, dynamin 2 (Dyn 2) associates predominantly with clathrin-coated vesicles at the plasma membrane and the Golgi apparatus. Upon treatment with PDGF to induce cell migration, dynamin becomes markedly associated with membrane ruffles and lamellipodia. Biochemical and morphological studies using antibodies and GFP-tagged dynamin demonstrate an interaction with cortactin, Cortactin is an actin-binding protein that contains a well defined SH3 domain. Using a variety of biochemical methods we demonstrate that the cortactin-SH3 domain associates with the proline-rich domain (PRD) of dynamin. Functional studies that express wild-type and mutant forms of dynamin and/or cortactin in living cells support these in vitro observations and demonstratethat an increased expression of cortactin leads to a significant recruitment of endogenous or expressed dynamin into the cell ruffle. Further, expression of a cortactin protein lacking the interactive SH3 domain (Cort Delta SH3) significantly reduces dynamin localization to the ruffle. Accordingly,transfected cells expressing Dyn 2 lacking the PRD (Dyn 2(aa)Delta PRD) sequester little of this protein to the cortactin-rich ruffle. Interestingly,these mutant cells are viable, but display dramatic alterations in morphology. This change in shape appears to be due, in part, to a striking increase in the number of actin stress fibers. These findings provide the first demonstration that dynamin can interact with the actin cytoskeleton to regulate actin reorganization and subsequently cell shape.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/01/21 alle ore 02:39:58