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Volumn 15, Issue 1, 2003, Pages 31-39

Dynamin at the actin-membrane interface

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ACTIN BINDING PROTEIN; ACTIN RELATED PROTEIN 2; ACTIN RELATED PROTEIN 3; CELL ENZYME; CELL PROTEIN; CORTACTIN; DYNAMIN; GROWTH FACTOR RECEPTOR BOUND PROTEIN 2; INTERSECTIN; MYOSIN; NUCLEOTIDE; POLYMER; PROFILIN; PROLINE; PROTEIN ABP1; PROTEIN NCK; SYNDAPIN; UNCLASSIFIED DRUG; WISKOTT ALDRICH SYNDROME PROTEIN;

EID: 0037223126     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(02)00010-8     Document Type: Review
Times cited : (208)

References (59)
  • 1
    • 0034784987 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of dynamin in the constricted state
    • Zhang P., Hinshaw J.E. Three-dimensional reconstruction of dynamin in the constricted state. Nat. Cell Biol. 3:2001;922-926.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 922-926
    • Zhang, P.1    Hinshaw, J.E.2
  • 3
    • 0034597062 scopus 로고    scopus 로고
    • Interactions between dynamin and the actin binding protein cortactin modulate cell shape
    • McNiven M.A., Kim L., Krueger E.W., Orth J.D., Cao H., Wong T.W. Interactions between dynamin and the actin binding protein cortactin modulate cell shape. J. Cell Biol. 151:2000;187-198.
    • (2000) J. Cell Biol. , vol.151 , pp. 187-198
    • McNiven, M.A.1    Kim, L.2    Krueger, E.W.3    Orth, J.D.4    Cao, H.5    Wong, T.W.6
  • 4
    • 0037039431 scopus 로고    scopus 로고
    • Dynamin at actin tails
    • ••] demonstrate that dynamin localizes to Listeria and vesicular actin comets, and regulates their formation, velocity and movement. The proline/arginine-rich domain (PRD) of dynamin is important for efficient targeting of dynamin to the comet structures, as dynamin lacking the PRD did not effectively localize. These data suggest that dynamin regulates actin polymerization at the actin-membrane interface to mediate the actin-dependent forward movement of membranes.
    • ••] demonstrate that dynamin localizes to Listeria and vesicular actin comets, and regulates their formation, velocity and movement. The proline/arginine-rich domain (PRD) of dynamin is important for efficient targeting of dynamin to the comet structures, as dynamin lacking the PRD did not effectively localize. These data suggest that dynamin regulates actin polymerization at the actin-membrane interface to mediate the actin-dependent forward movement of membranes.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 161-166
    • Lee, E.1    De Camilli, P.2
  • 7
    • 0032481313 scopus 로고    scopus 로고
    • In mouse brain profilin I and profilin II associate with regulators of the endocytic pathway and actin assembly
    • Witke W., Podtelejnikov A.V., Di Nardo A., Sutherland J.D., Gurniak C.B., Dott C., Mann M. In mouse brain profilin I and profilin II associate with regulators of the endocytic pathway and actin assembly. EMBO J. 17:1998;967-976.
    • (1998) EMBO J. , vol.17 , pp. 967-976
    • Witke, W.1    Podtelejnikov, A.V.2    Di Nardo, A.3    Sutherland, J.D.4    Gurniak, C.B.5    Dott, C.6    Mann, M.7
  • 12
    • 0035897420 scopus 로고    scopus 로고
    • Mammalian Abp1, a signal-responsive F-actin-binding protein, links the actin cytoskeleton to endocytosis via the GTPase dynamin
    • This study identified Abp1 as a direct binding partner of dynamin. The data show that Abp1 has a role in clathrin-mediated endocytosis and that the interactions of Abp1 with F-actin and dynamin are important for this function. Abp1 also co-localized with dynamin in actin-rich sites in primary hippocampal neurons, suggesting that these proteins may possibly function together in neurons.
    • Kessels M.M., Engqvist-Goldstein A.E.Y., Drubin D.G., Qualmann B. Mammalian Abp1, a signal-responsive F-actin-binding protein, links the actin cytoskeleton to endocytosis via the GTPase dynamin. J. Cell Biol. 153:2001;351-366 This study identified Abp1 as a direct binding partner of dynamin. The data show that Abp1 has a role in clathrin-mediated endocytosis and that the interactions of Abp1 with F-actin and dynamin are important for this function. Abp1 also co-localized with dynamin in actin-rich sites in primary hippocampal neurons, suggesting that these proteins may possibly function together in neurons.
    • (2001) J. Cell Biol. , vol.153 , pp. 351-366
    • Kessels, M.M.1    Engqvist-Goldstein, A.E.Y.2    Drubin, D.G.3    Qualmann, B.4
  • 13
    • 0033980106 scopus 로고    scopus 로고
    • Association of mouse actin-binding protein 1 (mAbp1/SH3P7), an Src kinase target, with dynamic regions of the cortical actin cytoskeleton in response to Rac1 activation
    • Kessels M.M., Engqvist-Goldstein A.E.Y., Drubin D.G. Association of mouse actin-binding protein 1 (mAbp1/SH3P7), an Src kinase target, with dynamic regions of the cortical actin cytoskeleton in response to Rac1 activation. Mol. Biol. Cell. 11:2000;393-412.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 393-412
    • Kessels, M.M.1    Engqvist-Goldstein, A.E.Y.2    Drubin, D.G.3
  • 14
    • 0036179523 scopus 로고    scopus 로고
    • Golgi vesicle proteins are linked to the assembly of an actin complex defined by mAbp1A
    • As with clathrin pits and clathrin-mediated endocytosis, Abp1 is shown to localize to the Golgi and to function during the formation of Golgi-derived vesicles that are transported to the plasma membrane. Further, Abp1 binding to F-actin on the Golgi appears dependent on Arp2/3-mediated actin polymerization.
    • Fucini R., Chen J., Sharma C., Kessels M., Stamnes M. Golgi vesicle proteins are linked to the assembly of an actin complex defined by mAbp1A. Mol. Biol. Cell. 13:2002;621-631 As with clathrin pits and clathrin-mediated endocytosis, Abp1 is shown to localize to the Golgi and to function during the formation of Golgi-derived vesicles that are transported to the plasma membrane. Further, Abp1 binding to F-actin on the Golgi appears dependent on Arp2/3-mediated actin polymerization.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 621-631
    • Fucini, R.1    Chen, J.2    Sharma, C.3    Kessels, M.4    Stamnes, M.5
  • 19
    • 0034611006 scopus 로고    scopus 로고
    • Syndapin isoforms participate in receptor-mediated endocytosis and actin organization
    • Qualmann B., Kelly R.B. Syndapin isoforms participate in receptor-mediated endocytosis and actin organization. J. Cell Biol. 148:2000;1047-1061.
    • (2000) J. Cell Biol. , vol.148 , pp. 1047-1061
    • Qualmann, B.1    Kelly, R.B.2
  • 23
    • 0032890318 scopus 로고    scopus 로고
    • Characterization of interactions of Nck with Sos and dynamin
    • Wunderlich L., Farago A., Buday L. Characterization of interactions of Nck with Sos and dynamin. Cell Signal. 11:1999;25-29.
    • (1999) Cell Signal , vol.11 , pp. 25-29
    • Wunderlich, L.1    Farago, A.2    Buday, L.3
  • 25
    • 0035854732 scopus 로고    scopus 로고
    • Nck and phosphatidylinositol 4,5-bisphosphate synergistically activate actin polymerization through the N-WASP-Arp2/3 pathway
    • Rohatgi R., Nollau P., Ho H.H., Kirschner M.W., Mayer B.J. Nck and phosphatidylinositol 4,5-bisphosphate synergistically activate actin polymerization through the N-WASP-Arp2/3 pathway. J. Biol. Chem. 276:2001;26448-26452.
    • (2001) J. Biol. Chem. , vol.276 , pp. 26448-26452
    • Rohatgi, R.1    Nollau, P.2    Ho, H.H.3    Kirschner, M.W.4    Mayer, B.J.5
  • 27
    • 0037020265 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate (PIP2)-induced vesicle movement depends on N-WASP and involves Nck, WIP, and Grb2
    • Benesch S., Lommel S., Steffen A., Stradal T.E.B., Scaplehorn N., Way M., Wehland J., Rottner K. Phosphatidylinositol 4,5-bisphosphate (PIP2)-induced vesicle movement depends on N-WASP and involves Nck, WIP, and Grb2. J. Biol. Chem. 277:2002;37771-37776.
    • (2002) J. Biol. Chem. , vol.277 , pp. 37771-37776
    • Benesch, S.1    Lommel, S.2    Steffen, A.3    Stradal, T.E.B.4    Scaplehorn, N.5    Way, M.6    Wehland, J.7    Rottner, K.8
  • 28
    • 0033578374 scopus 로고    scopus 로고
    • Wiskott-Aldrich syndrome protein regulates podosomes in primary human macrophages
    • Linder S., Nelson D., Weiss M., Aepfelbacher M. Wiskott-Aldrich syndrome protein regulates podosomes in primary human macrophages. Proc. Natl. Acad. Sci. U.S.A. 96:1999;9648-9653.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 9648-9653
    • Linder, S.1    Nelson, D.2    Weiss, M.3    Aepfelbacher, M.4
  • 29
    • 0036195293 scopus 로고    scopus 로고
    • A selective inhibitor of matrix metalloproteinases inhibits the migration of isolated osteoclasts by increasing the life span of podosomes
    • Goto T., Maeda H., Tanaka T. A selective inhibitor of matrix metalloproteinases inhibits the migration of isolated osteoclasts by increasing the life span of podosomes. J. Bone Miner. Metab. 20:2002;98-105.
    • (2002) J. Bone Miner. Metab. , vol.20 , pp. 98-105
    • Goto, T.1    Maeda, H.2    Tanaka, T.3
  • 30
    • 0033527066 scopus 로고    scopus 로고
    • An invasion-related complex of cortactin, paxillin and PKCμ associates with invadopodia at sites of extracellular matrix degradation
    • Bowden E.T., Barth M., Thomas D., Glazer R.I., Mueller S.C. An invasion-related complex of cortactin, paxillin and PKCμ associates with invadopodia at sites of extracellular matrix degradation. Oncogene. 18:1999;4440-4449.
    • (1999) Oncogene , vol.18 , pp. 4440-4449
    • Bowden, E.T.1    Barth, M.2    Thomas, D.3    Glazer, R.I.4    Mueller, S.C.5
  • 31
    • 0035864376 scopus 로고    scopus 로고
    • MT1-MMP initiates activation of pro-MMP-2 and integrin alphsvbeta3 promotes maturation of MMP2 in breast carcinoma cells
    • Deryugina E.I., Ratnikov B., Monosov E., Postnova T.I., DiScipio R., Smith J.W., Strongin A.Y. MT1-MMP initiates activation of pro-MMP-2 and integrin alphsvbeta3 promotes maturation of MMP2 in breast carcinoma cells. Exp. Cell Res. 263:2001;209-223.
    • (2001) Exp. Cell Res. , vol.263 , pp. 209-223
    • Deryugina, E.I.1    Ratnikov, B.2    Monosov, E.3    Postnova, T.I.4    DiScipio, R.5    Smith, J.W.6    Strongin, A.Y.7
  • 33
    • 0034282711 scopus 로고    scopus 로고
    • Scar/WAVE-1, a Wiskott-Aldrich syndrome protein, assembles an actin-associated multi-kinase scaffold
    • Westphal R.S., Soderling S.H., Alto N.M., Langeberg L.K., Scott J.D. Scar/WAVE-1, a Wiskott-Aldrich syndrome protein, assembles an actin-associated multi-kinase scaffold. EMBO J. 19:2000;4589-4600.
    • (2000) EMBO J. , vol.19 , pp. 4589-4600
    • Westphal, R.S.1    Soderling, S.H.2    Alto, N.M.3    Langeberg, L.K.4    Scott, J.D.5
  • 34
    • 0022357441 scopus 로고
    • Rous sarcoma virus-transformed fibroblasts adhere primarily at discrete protrusions of the ventral membrane called podosomes
    • Tarone G., Cirillo D., Giancotti F.G., Comoglio P.M., Marchisio P.C. Rous sarcoma virus-transformed fibroblasts adhere primarily at discrete protrusions of the ventral membrane called podosomes. Exp. Cell Res. 159:1985;141-157.
    • (1985) Exp. Cell Res. , vol.159 , pp. 141-157
    • Tarone, G.1    Cirillo, D.2    Giancotti, F.G.3    Comoglio, P.M.4    Marchisio, P.C.5
  • 35
    • 0032516055 scopus 로고    scopus 로고
    • Src interacts with dynamin and synapsin in neuronal cells
    • Foster-Barber A., Bishop J.M. Src interacts with dynamin and synapsin in neuronal cells. Proc. Natl. Acad. Sci. U.S.A. 95:1998;4673-4677.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 4673-4677
    • Foster-Barber, A.1    Bishop, J.M.2
  • 36
    • 0033555946 scopus 로고    scopus 로고
    • Src-mediated tyrosine phosphorylation of dynamin is required for beta2-adrenergic receptor internalization and mitogen-activated protein kinase signaling
    • Ahn S., Maudsley S., Luttrell L.M., Lefkowitz R.J., Daaka Y. Src-mediated tyrosine phosphorylation of dynamin is required for beta2-adrenergic receptor internalization and mitogen-activated protein kinase signaling. J. Biol. Chem. 274:1999;1185-1188.
    • (1999) J. Biol. Chem. , vol.274 , pp. 1185-1188
    • Ahn, S.1    Maudsley, S.2    Luttrell, L.M.3    Lefkowitz, R.J.4    Daaka, Y.5
  • 37
    • 0027419589 scopus 로고
    • src substrate, is a filamentous actin-binding protein enriched in the cell cortex
    • src substrate, is a filamentous actin-binding protein enriched in the cell cortex. J. Cell Biol. 120:1993;1417-1426.
    • (1993) J. Cell Biol. , vol.120 , pp. 1417-1426
    • Wu, H.1    Parsons, J.T.2
  • 38
    • 0036633295 scopus 로고    scopus 로고
    • The endocytic machinery at an interface with the actin cytoskeleton: A dynamic, hip intersection
    • McPherson P.S. The endocytic machinery at an interface with the actin cytoskeleton: a dynamic, hip intersection. Trends Cell Biol. 12:2002;312-315.
    • (2002) Trends Cell Biol. , vol.12 , pp. 312-315
    • McPherson, P.S.1
  • 39
    • 0036702196 scopus 로고    scopus 로고
    • Regulating the actin cytoskeleton during vesicular transport
    • Stamnes M. Regulating the actin cytoskeleton during vesicular transport. Curr. Opin. Cell Biol. 14:2002;428-433.
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 428-433
    • Stamnes, M.1
  • 41
    • 0037134014 scopus 로고    scopus 로고
    • Local actin polymerization and dynamin recruitment in SV40-induced internalization of caveolae
    • This study followed caveolae-mediated SV40 internalization in real-time and showed that dynamin was transiently recruited to the SV40-docked caveolae in a tyrosine-kinase-dependent manner, and that actin tails polymerized at the caveolae, resulting in the internalization of the virus. GTPase-deficient mutant dynamin blocked the internalization of SV40. Interestingly, wild-type dynamin showed a 'blinking' phenomena at the caveolae, while GTPase-deficient dynamin did not.
    • Pelkmans L., Puntener D., Helenius A. Local actin polymerization and dynamin recruitment in SV40-induced internalization of caveolae. Science. 296:2002;535-539 This study followed caveolae-mediated SV40 internalization in real-time and showed that dynamin was transiently recruited to the SV40-docked caveolae in a tyrosine-kinase-dependent manner, and that actin tails polymerized at the caveolae, resulting in the internalization of the virus. GTPase-deficient mutant dynamin blocked the internalization of SV40. Interestingly, wild-type dynamin showed a 'blinking' phenomena at the caveolae, while GTPase-deficient dynamin did not.
    • (2002) Science , vol.296 , pp. 535-539
    • Pelkmans, L.1    Puntener, D.2    Helenius, A.3
  • 42
    • 0036714223 scopus 로고    scopus 로고
    • Imaging actin and dynamin recruitment during invagination of single clathrin-coated pits
    • ••], dynamin was found to 'blink' while being recruited; however, just before accumulation of actin, the dynamin spot became substantially brighter. These results support a model where dynamin is recruited to the necks of vesicles, where it probably functions to pinch the neck and stimulate actin polymerization at the actin-membrane interface. The recruitment of dynamin mutants, and their affect on the 'burst' of actin accumulation at the membrane interface was not studied.
    • ••], dynamin was found to 'blink' while being recruited; however, just before accumulation of actin, the dynamin spot became substantially brighter. These results support a model where dynamin is recruited to the necks of vesicles, where it probably functions to pinch the neck and stimulate actin polymerization at the actin-membrane interface. The recruitment of dynamin mutants, and their affect on the 'burst' of actin accumulation at the membrane interface was not studied.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 691-698
    • Merrifield, C.J.1    Feldman, M.E.2    Wan, L.3    Almers, W.4
  • 43
    • 0034503124 scopus 로고    scopus 로고
    • All three PACSIN isoforms bind to endocytic proteins and inhibit endocytosis
    • Modregger J., Ritter B., Witter B., Paulsson M., Plomann M. All three PACSIN isoforms bind to endocytic proteins and inhibit endocytosis. J. Cell Sci. 113:2000;4511-4521.
    • (2000) J. Cell Sci. , vol.113 , pp. 4511-4521
    • Modregger, J.1    Ritter, B.2    Witter, B.3    Paulsson, M.4    Plomann, M.5
  • 44
    • 0029942238 scopus 로고    scopus 로고
    • Association of a dynamin-like protein with the Golgi apparatus in mammalian cells
    • Henley J.R., McNiven M.A. Association of a dynamin-like protein with the Golgi apparatus in mammalian cells. J. Cell Biol. 133:1996;761-775.
    • (1996) J. Cell Biol. , vol.133 , pp. 761-775
    • Henley, J.R.1    McNiven, M.A.2
  • 46
    • 0032559342 scopus 로고    scopus 로고
    • Role of dynamin in the formation of transport vesicles from the trans-Golgi network
    • Jones S.M., Howell K.E., Henley J.R., Cao H., McNiven M.A. Role of dynamin in the formation of transport vesicles from the trans-Golgi network. Science. 279:1998;573-577.
    • (1998) Science , vol.279 , pp. 573-577
    • Jones, S.M.1    Howell, K.E.2    Henley, J.R.3    Cao, H.4    McNiven, M.A.5
  • 47
    • 0036153898 scopus 로고    scopus 로고
    • Dynamin-dependent transferrin receptor recycling by endosome-derived clathrin-coated vesicles
    • van Dam E.M., Stoorvogel W. Dynamin-dependent transferrin receptor recycling by endosome-derived clathrin-coated vesicles. Mol. Biol. Cell. 13:2002;169-182.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 169-182
    • Van Dam, E.M.1    Stoorvogel, W.2
  • 48
  • 50
    • 17144439652 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate induces actin-based movement of raft-enriched vesicles through WASP-Arp2/3
    • The transient expression of type I phosphatidylinositol phosphate 5-kinase resulted in the accumulation of phosphatidylinositol 4,5-bisphosphate and the formation of vesicle comets that form from cholesterol-rich microdomains in the plasma membrane, and from the Golgi. Comet formation was influenced by activating tyrosine kinases, and the 'heads' of the comets were enriched in phosphotyrosines. These vesicle comets used the WASP-Arp2/3 machinery to induce actin polymerization and the propulsion of the membrane vesicle.
    • Rozelle A.L., Machesky L.M., Yamamoto M., Driessens M.H.E., Insall R.H., Roth M.G., Luby-Phelps K., Marriott G., Hall A., Yin H.L. Phosphatidylinositol 4,5-bisphosphate induces actin-based movement of raft-enriched vesicles through WASP-Arp2/3. Curr. Biol. 10:2000;311-320 The transient expression of type I phosphatidylinositol phosphate 5-kinase resulted in the accumulation of phosphatidylinositol 4,5-bisphosphate and the formation of vesicle comets that form from cholesterol-rich microdomains in the plasma membrane, and from the Golgi. Comet formation was influenced by activating tyrosine kinases, and the 'heads' of the comets were enriched in phosphotyrosines. These vesicle comets used the WASP-Arp2/3 machinery to induce actin polymerization and the propulsion of the membrane vesicle.
    • (2000) Curr. Biol. , vol.10 , pp. 311-320
    • Rozelle, A.L.1    Machesky, L.M.2    Yamamoto, M.3    Driessens, M.H.E.4    Insall, R.H.5    Roth, M.G.6    Luby-Phelps, K.7    Marriott, G.8    Hall, A.9    Yin, H.L.10
  • 53
    • 0037128213 scopus 로고    scopus 로고
    • Purification of pseudopodia from polarized cells reveals redistribution and activation of Rac through assembly of a CAS/Crk scaffold
    • Cho S.Y., Klemke R.L. Purification of pseudopodia from polarized cells reveals redistribution and activation of Rac through assembly of a CAS/Crk scaffold. J. Cell Biol. 156:2002;725-736.
    • (2002) J. Cell Biol. , vol.156 , pp. 725-736
    • Cho, S.Y.1    Klemke, R.L.2
  • 54
    • 0034597092 scopus 로고    scopus 로고
    • Cortactin localization to sites of actin assembly in lamellipodia requires interactions with F-Actin and the Arp2/3 complex
    • Weed S.A., Karginov A.V., Schafer D.A., Weaver A.M., Kinley A.W., Cooper J.A., Parsons J.T. Cortactin localization to sites of actin assembly in lamellipodia requires interactions with F-Actin and the Arp2/3 complex. J. Cell Biol. 151:2000;29-40.
    • (2000) J. Cell Biol. , vol.151 , pp. 29-40
    • Weed, S.A.1    Karginov, A.V.2    Schafer, D.A.3    Weaver, A.M.4    Kinley, A.W.5    Cooper, J.A.6    Parsons, J.T.7
  • 56
    • 0033623198 scopus 로고    scopus 로고
    • Nckβ adapter regulates actin polymerization in NIH 3T3 fibroblasts in response to platelet-derived growth factor bb
    • Chen M., She H., Kim A., Woodley D.T., Li W. Nckβ adapter regulates actin polymerization in NIH 3T3 fibroblasts in response to platelet-derived growth factor bb. Mol. Cell Biol. 20:2000;7867-7880.
    • (2000) Mol. Cell Biol. , vol.20 , pp. 7867-7880
    • Chen, M.1    She, H.2    Kim, A.3    Woodley, D.T.4    Li, W.5
  • 58
    • 17344380140 scopus 로고    scopus 로고
    • Role of phosphatidylinositol 4,5-bisphosphate in Ras/Rac-induced disruption of the cortactin-actomyosin complex and malignant transformation
    • He H., Watanabe T., Zhan X., Huang C., Schuuring E., Fukami K., Takenawa T., Kumar C.C., Simpson R.J., Maruta H. Role of phosphatidylinositol 4,5-bisphosphate in Ras/Rac-induced disruption of the cortactin-actomyosin complex and malignant transformation. Mol. Cell Biol. 18:1998;3829-3837.
    • (1998) Mol. Cell Biol. , vol.18 , pp. 3829-3837
    • He, H.1    Watanabe, T.2    Zhan, X.3    Huang, C.4    Schuuring, E.5    Fukami, K.6    Takenawa, T.7    Kumar, C.C.8    Simpson, R.J.9    Maruta, H.10
  • 59
    • 0037371802 scopus 로고    scopus 로고
    • Cortactin is a component of clathrin-coated pits and participates in receptor-mediated endocytosis
    • in press
    • Cao H, Orth JD, Chen J, Weller SG, Heuser JE, McNiven MA: Cortactin is a component of clathrin-coated pits and participates in receptor-mediated endocytosis. Mol Cell Biol 2003, in press.
    • (2003) Mol Cell Biol
    • Cao, H.1    Orth, J.D.2    Chen, J.3    Weller, S.G.4    Heuser, J.E.5    McNiven, M.A.6


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