Cell motility and the cytoskeleton最新文献_第3页

Actin and alpha-actinin dynamics in the adhesion and motility of EPEC and EHEC on host cells. 肌动蛋白和α -肌动蛋白在EPEC和EHEC对宿主细胞的粘附和运动中的动力学。

Cell motility and the cytoskeleton Pub Date : 2005-02-01 DOI: 10.1002/cm.20047

Nathan C Shaner, Joseph W Sanger, Jean M Sanger

{"title":"Actin and alpha-actinin dynamics in the adhesion and motility of EPEC and EHEC on host cells.","authors":"Nathan C Shaner, Joseph W Sanger, Jean M Sanger","doi":"10.1002/cm.20047","DOIUrl":"https://doi.org/10.1002/cm.20047","url":null,"abstract":"Two pathogenic Escherichia coli, Enteropathogenic E. coli (EPEC) and Enterohemorrhagic E. coli (EHEC), adhere to the outside of host cells and induce cytoskeletal rearrangements leading to the formation of membrane-encased pedestals comprised of actin filaments and other associated proteins beneath the bacteria. The structure of the pedestals induced by the two pathogens appears similar, although those induced by EHEC are shorter in length. Fluorescence Recovery After Photobleaching (FRAP) was used to determine potential differences of actin polymerization in EPEC and EHEC induced pedestals in cultured PtK2 cells expressing either Green or Yellow Fluorescent Protein (GFP or YFP) fused to actin or alpha-actinin. When all the fluorescent actin in a pedestal on EPEC-infected cells was photobleached, fluorescence recovery first occurred directly beneath the bacterium in a band that grew wider at a rate of one micron/minute. Consistently observed in all EPEC-induced pedestals, whether they were stationary, lengthening, or translocating, the rate of actin polymerization that occurred at the pedestal tip was approximately 1 mum/min. Overall, a much slower rate of actin polymerization was measured in long EHEC-induced pedestals. In contrast to the dynamics of GFP-actin, recovery of GFP-alpha-actinin fluorescence was not polarized, with the actin cross-linking protein exchanging all the length of the EPEC/EHEC induced pedestals. Surprisingly, the depolymerization and retrograde flow of pedestal actin, as well as pedestal translocations, were inhibited reversibly by either 2,3-butanedione monoxime (BDM) or by a combination of sodium azide and 2-deoxy D-glucose, leading to an increase in the lengths of the pedestals. A simple physical model was developed to describe elongation and translocation of EPEC/EHEC pedestals in terms of actin polymerization and depolymerization dynamics.","PeriodicalId":9675,"journal":{"name":"Cell motility and the cytoskeleton","volume":"60 2","pages":"104-20"},"PeriodicalIF":0.0,"publicationDate":"2005-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1002/cm.20047","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"24884082","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 34

Dynamics of endocytic traffic of Entamoeba histolytica revealed by confocal microscopy and flow cytometry. 用共聚焦显微镜和流式细胞术观察溶组织内阿米巴的内吞动力学。

Cell motility and the cytoskeleton Pub Date : 2004-12-01 DOI: 10.1002/cm.20038

Isaura Meza, Margaret Clarke

{"title":"Dynamics of endocytic traffic of Entamoeba histolytica revealed by confocal microscopy and flow cytometry.","authors":"Isaura Meza, Margaret Clarke","doi":"10.1002/cm.20038","DOIUrl":"https://doi.org/10.1002/cm.20038","url":null,"abstract":"Entamoeba histolytica, the protozoan parasite of humans, manifests constitutive endocytosis to obtain nutrients and, when induced to express invasive behavior, as a means of ingesting and processing host cells and tissue debris. E. histolytica trophozoites were grown in liquid axenic medium that contained fluorescently labeled fluid-phase markers, so that the kinetics of uptake, the transit of loaded endosomes through the cytoplasm, and the time of release of the markers could be monitored by flow cytometry. Confocal microscopy of live trophozoites revealed uptake of fluid by avid macropinocytosis and the occurrence of fusion between young and older endosomes, as well as between pinosomes and phagosomes containing bacteria. Endosomes were rapidly acidified, then gradually neutralized; finally, indigestible material was released. Transit of endosomes containing fluid-phase markers required about 2 h. Uptake and release of fluid-phase markers were impaired by drugs that inhibited actin dynamics and actin-myosin interaction; uptake was also impaired by inhibition of PI 3-kinase. A striking feature of the trophozoites was the great heterogeneity of their endocytic behavior.","PeriodicalId":9675,"journal":{"name":"Cell motility and the cytoskeleton","volume":" ","pages":"215-26"},"PeriodicalIF":0.0,"publicationDate":"2004-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1002/cm.20038","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40913607","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 29

Aurora-C kinase is a novel chromosomal passenger protein that can complement Aurora-B kinase function in mitotic cells. Aurora-C激酶是一种新的染色体乘客蛋白，可以补充有丝分裂细胞中Aurora-B激酶的功能。

Cell motility and the cytoskeleton Pub Date : 2004-12-01 DOI: 10.1002/cm.20039

Kaori Sasai, Hiroshi Katayama, David L Stenoien, Satoshi Fujii, Reiko Honda, Masashi Kimura, Yukio Okano, Masaaki Tatsuka, Fumio Suzuki, Erich A Nigg, William C Earnshaw, William R Brinkley, Subrata Sen

{"title":"Aurora-C kinase is a novel chromosomal passenger protein that can complement Aurora-B kinase function in mitotic cells.","authors":"Kaori Sasai, Hiroshi Katayama, David L Stenoien, Satoshi Fujii, Reiko Honda, Masashi Kimura, Yukio Okano, Masaaki Tatsuka, Fumio Suzuki, Erich A Nigg, William C Earnshaw, William R Brinkley, Subrata Sen","doi":"10.1002/cm.20039","DOIUrl":"https://doi.org/10.1002/cm.20039","url":null,"abstract":"The function of Aurora-C kinase, a member of the Aurora kinase family identified in mammals, is currently unknown. We present evidence that Aurora-C, like Aurora-B kinase, is a chromosomal passenger protein localizing first to centromeres and then to the midzone of mitotic cells. Aurora-C transcript is expressed at a moderate level albeit about an order of magnitude lower than Aurora-B transcript in diploid human fibroblasts. The level of Aurora-C transcript is elevated in several human cancer cell types. Aurora-C and Aurora-B mRNA and protein expressions are maximally elevated during the G2/M phase but their expression profiles in synchronized cells reveal differential temporal regulation through the cell cycle with Aurora-C level peaking after that of Aurora-B during the later part of the M phase. Aurora-C, like Aurora-B, interacts with the inner centromere protein (INCENP) at the carboxyl terminal end spanning the conserved IN box domain. Competition binding assays and transfection experiments revealed that, compared with Aurora-C, Aurora-B has preferential binding affinity to INCENP and co-expression of the two in vivo interferes with INCENP binding, localization, and stability of these proteins. A kinase-dead mutant of Aurora-C had a dominant negative effect inducing multinucleation in a dose-dependent manner. siRNA mediated silencing of Aurora-C and Aurora-B also gave rise to multinucleated cells with the two kinases silenced at the same time displaying an additive effect. Finally, Aurora-C could rescue the Aurora-B silenced multinucleation phenotype, demonstrating that Aurora-C kinase function overlaps with and complements Aurora-B kinase function in mitosis.","PeriodicalId":9675,"journal":{"name":"Cell motility and the cytoskeleton","volume":"59 4","pages":"249-63"},"PeriodicalIF":0.0,"publicationDate":"2004-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1002/cm.20039","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"24776158","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 270

Sphingosine-1-phosphate plays a role in the suppression of lateral pseudopod formation during Dictyostelium discoideum cell migration and chemotaxis. 鞘氨醇-1-磷酸在盘齿钢鞘细胞迁移和趋化过程中抑制侧假足的形成中起作用。

Cell motility and the cytoskeleton Pub Date : 2004-12-01 DOI: 10.1002/cm.20035

Akhilesh Kumar, Deborah Wessels, Karla J Daniels, Hannah Alexander, Stephen Alexander, David R Soll

{"title":"Sphingosine-1-phosphate plays a role in the suppression of lateral pseudopod formation during Dictyostelium discoideum cell migration and chemotaxis.","authors":"Akhilesh Kumar, Deborah Wessels, Karla J Daniels, Hannah Alexander, Stephen Alexander, David R Soll","doi":"10.1002/cm.20035","DOIUrl":"https://doi.org/10.1002/cm.20035","url":null,"abstract":"Sphingosine-1-phosphate (S-1-P) is a bioactive lipid that plays a role in diverse biological processes. It functions both as an extracellular ligand through a family of high-affinity G-protein-coupled receptors, and intracellularly as a second messenger. A growing body of evidence has implicated S-1-P in controlling cell movement and chemotaxis in cultured mammalian cells. Mutant D. discoideum cells, in which the gene encoding the S-1-P lyase had been specifically disrupted by homologous recombination, previously were shown to be defective in pseudopod formation, suggesting that a resulting defect might exist in motility and/or chemotaxis. To test this prediction, we analyzed the behavior of mutant cells in buffer, and in both spatial and temporal gradients of the chemoattractant cAMP, using computer-assisted 2-D and 3-D motion analysis systems. Under all conditions, S-1-P lyase null mutants were unable to suppress lateral pseudopod formation like wild-type control cells. This resulted in a reduction in velocity in buffer and spatial gradients of cAMP. Mutant cells exhibited positive chemotaxis in spatial gradients of cAMP, but did so with lowered efficiency, again because of their inability to suppress lateral pseudopod formation. Mutant cells responded normally to simulated temporal waves of cAMP but mimicked the temporal dynamics of natural chemotactic waves. The effect must be intracellular since no homologs of the S-1-P receptors have been identified in the Dictyostelium genome. The defects in the S-1-P lyase null mutants were similar to those seen in mutants lacking the genes for myosin IA, myosin IB, and clathrin, indicating that S-1-P signaling may play a role in modulating the activity or organization of these cytoskeletal elements in the regulation of lateral pseudopod formation.","PeriodicalId":9675,"journal":{"name":"Cell motility and the cytoskeleton","volume":" ","pages":"227-41"},"PeriodicalIF":0.0,"publicationDate":"2004-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1002/cm.20035","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40913604","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 22

Cellular stiffness response to external deformation: tensional homeostasis in a single fibroblast. 细胞刚度对外部变形的响应:单个成纤维细胞的张力稳态。

Cell motility and the cytoskeleton Pub Date : 2004-12-01 DOI: 10.1002/cm.20037

Takeomi Mizutani, Hisashi Haga, Kazushige Kawabata

{"title":"Cellular stiffness response to external deformation: tensional homeostasis in a single fibroblast.","authors":"Takeomi Mizutani, Hisashi Haga, Kazushige Kawabata","doi":"10.1002/cm.20037","DOIUrl":"https://doi.org/10.1002/cm.20037","url":null,"abstract":"Stiffness responses of fibroblasts were measured by scanning probe microscopy, following elongation or compression by deformation of an elastic substrate by 8%. The cellular stiffness, reflecting intracellular tension acting along stress fibers, decreased or increased instantly in response to the elongating or compressing stimuli, respectively. After this rapid change, the fibroblasts gradually recovered to their initial stiffness during the following 2 h, and then stabilized. The cells did not show conspicuous changes in shape after the 8% deformation during the SPM measurements. Fluorescence examination for GFP-actin demonstrated that the structure of the stress fibers was not altered noticeably by this small degree of deformation. Treatment with Y-27632, to inhibit myosin phosphorylation and abrogate cellular contractility, eliminated the change in stiffness after the mechanical elongation. These results indicate that fibroblasts possess a mechanism that regulates intracellular tension along stress fibers to maintain the cellular stiffness in a constant equilibrium state.","PeriodicalId":9675,"journal":{"name":"Cell motility and the cytoskeleton","volume":"59 4","pages":"242-8"},"PeriodicalIF":0.0,"publicationDate":"2004-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1002/cm.20037","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"24768692","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 97

The tail of myosin reduces actin filament velocity in the in vitro motility assay. 在体外运动试验中，肌凝蛋白的尾部降低肌动蛋白丝的速度。

Cell motility and the cytoskeleton Pub Date : 2004-12-01 DOI: 10.1002/cm.20040

Bin Guo, William H Guilford

{"title":"The tail of myosin reduces actin filament velocity in the in vitro motility assay.","authors":"Bin Guo, William H Guilford","doi":"10.1002/cm.20040","DOIUrl":"https://doi.org/10.1002/cm.20040","url":null,"abstract":"It has been observed that heavy meromyosin (HMM) propels actin filaments to higher velocities than native myosin in the in vitro motility assay, yet the reason for this difference has remained unexplained. Since the major difference between these two proteins is the presence of the tail in native myosin, we tested the hypothesis that unknown interactions between actin and the tail (LMM) slow motility in native myosin. Chymotryptic HMM and LMM were mixed in a range of molar ratios (0-5 LMM/HMM) and compared to native rat skeletal myosin in the in vitro motility assay at 30 degrees C. Increasing proportions of LMM to HMM slowed actin filament velocities, becoming equivalent to native myosin at a ratio of 3 LMM/HMM. NH4+ -ATPase assays demonstrated that HMM concentrations on the surface were constant and independent of LMM concentration, arguing against a simple displacement mechanism. Relationships between velocity and the number of available heads suggested that the duty cycle of HMM was not altered by the presence of LMM. HMM prepared with a lower chymotrypsin concentration and with very short digestion times moved actin at the same high velocity. The difference between velocities of actin filament propelled by HMM and HMM/LMM decreased with increasing ionic strength, suggesting that ionic bonds between myosin tail and actin filaments may play a role in slowing filament velocity. These data suggest the high velocities of actin filaments over HMM result from the absence of drag generated by the myosin tail, and not from proteolytic nicking of the motor domain.","PeriodicalId":9675,"journal":{"name":"Cell motility and the cytoskeleton","volume":"59 4","pages":"264-72"},"PeriodicalIF":0.0,"publicationDate":"2004-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1002/cm.20040","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"24779886","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 44

Dephosphorylation of inner arm 1 is associated with ciliary reversals in Tetrahymena thermophila. 在嗜热四膜虫中，内臂1的去磷酸化与纤毛逆转有关。

Cell motility and the cytoskeleton Pub Date : 2004-02-01 DOI: 10.1002/cm.10158

Cassandra M Deckman, David G Pennock

{"title":"Dephosphorylation of inner arm 1 is associated with ciliary reversals in Tetrahymena thermophila.","authors":"Cassandra M Deckman, David G Pennock","doi":"10.1002/cm.10158","DOIUrl":"https://doi.org/10.1002/cm.10158","url":null,"abstract":"In many organisms, depolarizing stimuli cause an increase in intraciliary Ca2+, which results in reversal of ciliary beat direction and backward swimming. The mechanism by which an increase in intraciliary Ca2+ causes ciliary reversal is not known. Here we show that Tetrahymena cells treated with okadaic acid or cantharidin to inhibit protein phosphatases do not swim backwards in response to depolarizing stimuli. We also show that both okadaic acid and cantharidin inhibit backward swimming in reactivated, extracted cell models treated with Ca2+. In contrast, treatment of whole cells or extracted cell models with protein kinase inhibitors has no effect on backward swimming. These results suggest that a component of the axonemal machinery is dephosphorylated during ciliary reversal. The phosphorylation state of inner arm dynein 1 (I1) was determined before and after cells were exposed to depolarizing conditions that induce ciliary reversal. An I1 intermediate chain is phosphorylated in forward swimming cells but is dephosphorylated in cells treated with a depolarizing stimulus. Our results suggest that dephosphorylation of Tetrahymena inner arm dynein 1 may be an essential part of the mechanism of ciliary reversal in response to increased intraciliary Ca2+.","PeriodicalId":9675,"journal":{"name":"Cell motility and the cytoskeleton","volume":"57 2","pages":"73-83"},"PeriodicalIF":0.0,"publicationDate":"2004-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1002/cm.10158","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"24138439","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Maturation of DC is associated with changes in motile characteristics and adherence. DC的成熟与运动特征和依从性的改变有关。

Cell motility and the cytoskeleton Pub Date : 2004-02-01 DOI: 10.1002/cm.10163

Siobhan Burns, Samantha J Hardy, Joanna Buddle, Kwee L Yong, Gareth E Jones, Adrian J Thrasher

{"title":"Maturation of DC is associated with changes in motile characteristics and adherence.","authors":"Siobhan Burns, Samantha J Hardy, Joanna Buddle, Kwee L Yong, Gareth E Jones, Adrian J Thrasher","doi":"10.1002/cm.10163","DOIUrl":"https://doi.org/10.1002/cm.10163","url":null,"abstract":"Migration of dendritic cells (DC) from sentinel sites to lymphoid tissue entails the initiation and coordination of a complex series of cytoskeletal rearrangements resulting in polarised protrusion, formation of new adhesion points, and detachment. Although many diverse receptor-ligand interactions stimulating DC maturation and migration have been identified, the changes that occur in the structure of the actin cytoskeleton during these processes have received little attention. When derived in vitro, immature DC floated in clumps, and upon addition of maturation stimuli such as lipopolysaccharide (LPS), they rapidly adhered, developed polarity, and assembled actin-rich structures known as podosomes at the leading edge of the cell. Podosome assembly was associated with the specific recruitment of beta2 integrins, which in the absence of the Wiskott Aldrich Syndrome protein (WASp), did not occur. As maturation progressed, normal DC once again became rounded and devoid of podosomes. This change in morphology was closely associated with a quantitatively reduced ability to adhere to fibronectin or ICAM-1-coated surfaces. In immature DC, failure to form podosomes or selective inhibition of the CD18 component of podosomes resulted in a similarly reduced ability to adhere to ICAM-1, indicating that podosomes, through CD18, are necessary for tight adhesion to this ligand. We, therefore, propose that podosomes provide an essential link between directional cell protrusion and achievement of DC translocation by establishing new dynamic anchor points at the front of the cell. The temporal regulation of podosome assembly during DC maturation also suggests that they may be most critical for early movement, perhaps during transmigration of lymphatic endothelium.","PeriodicalId":9675,"journal":{"name":"Cell motility and the cytoskeleton","volume":"57 2","pages":"118-32"},"PeriodicalIF":0.0,"publicationDate":"2004-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1002/cm.10163","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"24138878","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 177

Myosin-mediated cytoskeleton contraction and Rho GTPases regulate laminin-5 matrix assembly. 肌球蛋白介导的细胞骨架收缩和Rho GTP酶调控层粘连蛋白-5基质的组装。

Cell motility and the cytoskeleton Pub Date : 2004-02-01 DOI: 10.1002/cm.10161

Gregory W DeHart, Jonathan C R Jones

{"title":"Myosin-mediated cytoskeleton contraction and Rho GTPases regulate laminin-5 matrix assembly.","authors":"Gregory W DeHart, Jonathan C R Jones","doi":"10.1002/cm.10161","DOIUrl":"10.1002/cm.10161","url":null,"abstract":"Laminin-5 is a major structural element of epithelial tissue basement membranes. In the matrix of cultured epithelial cells, laminin-5 is arranged into intricate patterns. Here we tested a hypothesis that myosin II-mediated actin contraction is necessary for the proper assembly of a laminin-5 matrix by cultured SCC12 epithelial cells. To do so, the cells were treated with ML-7, a myosin II light chain kinase inhibitor, or Y-27632, an inhibitor of Rho-kinase (ROCK), both of which block actomyosin contraction. Under these conditions, laminin-5 shows an aberrant localization in dense patches at the cell periphery. Since ROCK activity is regulated by the small GTPase Rho, this suggests that members of the Rho family of GTPases may also be important for laminin-5 matrix assembly by SCC12 cells. We confirmed this hypothesis since SCC12 cells expressing mutant proteins that inhibit RhoA, Rac, and Cdc42 assemble the same aberrant laminin-5 protein arrays as drug-treated cells. We have also evaluated the organization of the laminin-5 receptors alpha3beta1 and alpha6beta4 integrin and hemidesmosome proteins in ML-7- and Y-27632-treated cells or in cells in which RhoA, Rac, and Cdc42 activity were inhibited. In all instances, alpha3beta1 and alpha6beta4 integrin heterodimers, as well as hemidesmosome proteins, localize precisely with laminin-5 in the matrix of the cells. In summary, our results provide evidence that myosin II-mediated actin contraction and the activity of Rho GTPases are necessary for the proper organization of a laminin-5 matrix and localization of hemidesmosome protein arrays in epithelial cells.","PeriodicalId":9675,"journal":{"name":"Cell motility and the cytoskeleton","volume":"57 2","pages":"107-17"},"PeriodicalIF":0.0,"publicationDate":"2004-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1002/cm.10161","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"24138877","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 14

Overexpression of profilin reduces the migration of invasive breast cancer cells. profilin的过表达减少了浸润性乳腺癌细胞的迁移。

Cell motility and the cytoskeleton Pub Date : 2004-02-01 DOI: 10.1002/cm.10160

Partha Roy, Ken Jacobson

引用次数: 76