scholarly journals Networking galore: intermediate filaments and cell migration

2013 ◽  
Vol 25 (5) ◽  
pp. 600-612 ◽  
Author(s):  
Byung-Min Chung ◽  
Jeremy D Rotty ◽  
Pierre A Coulombe
Keyword(s):  
Cell Migration ◽  
Intermediate Filaments

scholarly journals Rudhira/BCAS3 couples microtubules and intermediate filaments to promote cell migration for angiogenic remodeling

2019 ◽  
Vol 30 (12) ◽  
pp. 1437-1450 ◽  
Author(s):  
Divyesh Joshi ◽  
Maneesha S. Inamdar
Keyword(s):  
Cell Migration ◽  
Intermediate Filaments ◽  
Cross Talk ◽  
Control Cell ◽  
The Novel ◽  
Mouse Development ◽  
Cytoskeleton Organization ◽  
Sprouting Angiogenesis ◽  
Promote Cell Migration ◽  
Necessary And Sufficient

Blood vessel formation requires endothelial cell (EC) migration that depends on dynamic remodeling of the cytoskeleton. Rudhira/Breast Carcinoma Amplified Sequence 3 (BCAS3) is a cytoskeletal protein essential for EC migration and sprouting angiogenesis during mouse development and is implicated in metastatic disease. Here, we report that Rudhira mediates cytoskeleton organization and dynamics during EC migration. Rudhira binds to both microtubules (MTs) and vimentin intermediate filaments (IFs) and stabilizes MTs. Rudhira depletion impairs cytoskeletal cross-talk, MT stability, and hence focal adhesion disassembly. The BCAS3 domain of Rudhira is necessary and sufficient for MT-IF cross-linking and cell migration. Pharmacologically restoring MT stability rescues gross cytoskeleton organization and angiogenic sprouting in Rudhira-depleted cells. Our study identifies the novel and essential role of Rudhira in cytoskeletal cross-talk and assigns function to the conserved BCAS3 domain. Targeting Rudhira could allow tissue-restricted cytoskeleton modulation to control cell migration and angiogenesis in development and disease.

scholarly journals Unidirectional Regulation of Vimentin Intermediate Filaments to Caveolin-1

2020 ◽  
Vol 21 (20) ◽  
pp. 7436
Author(s):  
Xuemeng Shi ◽  
Changyuan Fan ◽  
Yaming Jiu
Keyword(s):  
Cell Migration ◽  
Stress Response ◽  
Intermediate Filaments ◽  
Migration Rate ◽  
Osmotic Shock ◽  
Cellular Level ◽  
Caveolin 1 ◽  
Active Processes ◽  
Intracellular Motility ◽  
Vimentin Filaments

Both the mechanosensitive vimentin cytoskeleton and endocytic caveolae contribute to various active processes such as cell migration, morphogenesis, and stress response. However, the crosstalk between these two systems has remained elusive. Here, we find that the subcellular expression between vimentin and caveolin-1 is mutual exclusive, and vimentin filaments physically arrest the cytoplasmic motility of caveolin-1 vesicles. Importantly, vimentin depletion increases the phosphorylation of caveolin-1 on site Tyr14, and restores the compromised cell migration rate and directionality caused by caveolin-1 deprivation. Moreover, upon hypo-osmotic shock, vimentin-knockout recovers the reduced intracellular motility of caveolin-1 vesicles. In contrary, caveolin-1 depletion shows no effect on the expression, phosphorylation (on sites Ser39, Ser56, and Ser83), distribution, solubility, and cellular dynamics of vimentin filaments. Taken together, our data reveals a unidirectional regulation of vimentin to caveolin-1, at least on the cellular level.

Alpha-Catulin Co-Localizes With Vimentin Intermediate Filaments and Functions in Pulmonary Vascular Endothelial Cell Migration via ROCK

2015 ◽  
Vol 231 (4) ◽  
pp. 934-943 ◽  
Author(s):  
Michael D. Bear ◽  
Tiegang Liu ◽  
Shereen Abualkhair ◽  
Maher A. Ghamloush ◽  
Nicholas S. Hill ◽  
...  
Keyword(s):  
Cell Migration ◽  
Endothelial Cell ◽  
Intermediate Filaments ◽  
Vascular Endothelial Cell ◽  
Endothelial Cell Migration ◽  
Vascular Endothelial

scholarly journals APC binds intermediate filaments and is required for their reorganization during cell migration

2013 ◽  
Vol 200 (3) ◽  
pp. 249-258 ◽  
Author(s):  
Yasuhisa Sakamoto ◽  
Batiste Boëda ◽  
Sandrine Etienne-Manneville
Keyword(s):  
Cell Migration ◽  
Glial Fibrillary Acidic Protein ◽  
Intermediate Filaments ◽  
Carcinoma Cells ◽  
Adenomatous Polyposis ◽  
Polyposis Coli ◽  
Cellular Functions ◽  
Migration Assay ◽  
Armadillo Repeats

Intermediate filaments (IFs) are components of the cytoskeleton involved in most cellular functions, including cell migration. Primary astrocytes mainly express glial fibrillary acidic protein, vimentin, and nestin, which are essential for migration. In a wound-induced migration assay, IFs reorganized to form a polarized network that was coextensive with microtubules in cell protrusions. We found that the tumor suppressor adenomatous polyposis coli (APC) was required for microtubule interaction with IFs and for microtubule-dependent rearrangements of IFs during astrocyte migration. We also show that loss or truncation of APC correlated with the disorganization of the IF network in glioma and carcinoma cells. In migrating astrocytes, vimentin-associated APC colocalized with microtubules. APC directly bound polymerized vimentin via its armadillo repeats. This binding domain promoted vimentin polymerization in vitro and contributed to the elongation of IFs along microtubules. These results point to APC as a crucial regulator of IF organization and confirm its fundamental role in the coordinated regulation of cytoskeletons.

scholarly journals Rudhira/BCAS3 couples microtubules and intermediate filaments to promote cell migration for angiogenic remodeling

2018 ◽  
Author(s):  
Divyesh Joshi ◽  
Maneesha S. Inamdar
Keyword(s):  
Cell Migration ◽  
Intermediate Filaments ◽  
Control Cell ◽  
The Novel ◽  
Mouse Development ◽  
Cytoskeleton Organization ◽  
Sprouting Angiogenesis ◽  
Microtubule Stability ◽  
Promote Cell Migration ◽  
Necessary And Sufficient

AbstractBlood vessel formation requires endothelial cell (EC) migration that depends on dynamic remodeling of the cytoskeleton. Rudhira/Breast Carcinoma Amplified Sequence 3 (BCAS3) is a cytoskeletal protein essential for EC migration and sprouting angiogenesis during mouse development and implicated in metastatic disease. Here, we report that Rudhira mediates cytoskeleton organization and dynamics during EC migration. Rudhira binds to both microtubules and Vimentin intermediate filaments (IFs) and stabilizes microtubules. Rudhira depletion impairs cytoskeletal crosstalk, microtubule stability and hence focal adhesion disassembly. The BCAS3 domain of Rudhira is necessary and sufficient for microtubule-IF crosslinking and cell migration. Pharmacologically restoring microtubule stability rescues gross cytoskeleton organization and angiogenic sprouting in Rudhira depleted cells. Our study identifies the novel and essential role of Rudhira in cytoskeletal crosstalk and assigns function to the conserved BCAS3 domain. Targeting Rudhira could allow tissue-restricted cytoskeleton modulation to control cell migration and angiogenesis in development and disease.

scholarly journals Distinct Roles for CARMIL Isoforms in Cell Migration

2009 ◽  
Vol 20 (24) ◽  
pp. 5290-5305 ◽  
Author(s):  
Yun Liang ◽  
Hanspeter Niederstrasser ◽  
Marc Edwards ◽  
Charles E. Jackson ◽  
John A. Cooper
Keyword(s):  
Cell Migration ◽  
Intermediate Filaments ◽  
Molecular Mechanisms ◽  
Cultured Cells ◽  
The Other ◽  
Capping Protein ◽  
Myosin I ◽  
Conserved Genes ◽  
Phenotype Expression

Molecular mechanisms for cell migration, especially how signaling and cytoskeletal systems are integrated, are not understood well. Here, we examined the role of CARMIL (capping protein, Arp2/3, and Myosin-I linker) family proteins in migrating cells. Vertebrates express three conserved genes for CARMIL, and we examined the functions of the two CARMIL genes expressed in migrating human cultured cells. Both isoforms, CARMIL1 and 2, were necessary for cell migration, but for different reasons. CARMIL1 localized to lamellipodia and macropinosomes, and loss of its function caused loss of lamellipodial actin, along with defects in protrusion, ruffling, and macropinocytosis. CARMIL1-knockdown cells showed loss of activation of Rac1, and CARMIL1 was biochemically associated with the GEF Trio. CARMIL2, in contrast, colocalized with vimentin intermediate filaments, and loss of its function caused a distinctive multipolar phenotype. Loss of CARMIL2 also caused decreased levels of myosin-IIB, which may contribute to the polarity phenotype. Expression of one CARMIL isoform was not able to rescue the knockdown phenotypes of the other. Thus, the two isoforms are both important for cell migration, but they have distinct functions.

scholarly journals Epithelial cell migration requires the interaction between the vimentin and keratin intermediate filaments

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Cristina Velez-delValle ◽  
Meytha Marsch-Moreno ◽  
Federico Castro-Muñozledo ◽  
Ivan J. Galván-Mendoza ◽  
Walid Kuri-Harcuch
Keyword(s):  
Cell Migration ◽  
Epithelial Cell ◽  
Intermediate Filaments ◽  
Epithelial Cell Migration ◽  
Keratin Intermediate Filaments
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