Bridging cytoskeletal intersections

Fuchs, Elaine; Karakesisoglou, Iakowos

doi:10.1101/gad.861501

Cited by 146 publications

(105 citation statements)

References 91 publications

Supporting

Mentioning

102

Contrasting

Unclassified

Order By: Relevance

“…It is therefore likely that variations in the disassembly of keratin IFs observed in different types of epithelial cells are also regulated by keratin phosphorylation, along with the expression of unique keratin-associated proteins (Fuchs and Karakesisoglou, 2001;Leung et al, 2002). Because nestin does not appear to coassemble with keratin IFs in epithelial cell types such as those used in this study MDBK), proteins other than nestin are most likely responsive for their disassembly.…”

Section: Discussionmentioning

confidence: 95%

Nestin Promotes the Phosphorylation-dependent Disassembly of Vimentin Intermediate Filaments During Mitosis

Chou

Khuon

Herrmann

et al. 2003

MBoC

176

153

View full text Add to dashboard Cite

The expression of the intermediate filament (IF) protein nestin is closely associated with rapidly proliferating progenitor cells during neurogenesis and myogenesis, but little is known about its function. In this study, we examine the effects of nestin expression on the assembly state of vimentin IFs in nestin-free cells. Nestin is introduced by transient transfection and is positively correlated with the disassembly of vimentin IFs into nonfilamentous aggregates or particles in mitotic but not interphase cells. This nestin-mediated disassembly of IFs is dependent on the phosphorylation of vimentin by the maturation/M-phase–promoting factor at ser-55 in the amino-terminal head domain. In addition, the disassembly of vimentin IFs during mitosis appears to be a unique feature of nestin-expressing cell types. Furthermore, when the expression of nestin is downregulated by the nestin-specific small interfering RNA in nestin-expressing cells, vimentin IFs remain assembled throughout all stages of mitosis. Previous studies suggest that nonfilamentous vimentin particles are IF precursors and can be transported rapidly between different cytoplasmic compartments along microtubule tracks. On the basis of these observations, we speculate that nestin may play a role in the trafficking and distribution of IF proteins and potentially other cellular factors to daughter cells during progenitor cell division

show abstract

Section: Discussionmentioning

confidence: 95%

Nestin Promotes the Phosphorylation-dependent Disassembly of Vimentin Intermediate Filaments During Mitosis

Chou

Khuon

Herrmann

et al. 2003

MBoC

176

153

View full text Add to dashboard Cite

show abstract

“…In addition, we initiated a set of experiments to distinguish the role of the cytoskeleton in mechanosensation. Since the primary cilium is connected through the microtubule organizing center to the cytoplasmic microtubules, which are linked through membranous and nuclear proteins to the microfilaments and intermediate filaments (Fuchs and Karakesisoglou, 2001), the cilium adds to cytoskeletal deformation. Indeed, we demonstrate that the cytoskeletal microtubules are necessary to communicate biomechanical signals to the nucleus and induce gene expression.…”

Section: Introductionmentioning

confidence: 99%

Primary cilia sensitize endothelial cells for fluid shear stress

Hierck

Heiden

Alkemade

et al. 2008

Developmental Dynamics

159

108

View full text Add to dashboard Cite

Primary cilia are mechanosensors for fluid shear stress, and are involved in a number of syndromes and congenital anomalies. We identified endothelial cilia in areas of low shear stress in the embryonic heart. The objective of the present study was to demonstrate the role of primary cilia in mechanosensing. Ciliated embryonic endothelial cells were cultured from the heart, and non-ciliated cells from the arteries. Nonciliated cells that were subjected to fluid shear stress showed significantly less induction of the shear marker Krü ppel-Like Factor-2, as compared to ciliated cells. In addition, ciliated cells from which the cilia were chemically removed show a similar decrease in flow response. This shows that primary cilia sensitize endothelial cells for fluid shear stress. In addition, we targeted and stabilized the connection of the cilium to the cytoplasm by treatment with Colchicine and Taxol/Paclitaxel, respectively, and show that microtubular integrity is essential to sense shear stress. Developmental Dynamics 237:725-735, 2008.

show abstract

“…The family of proteins in which Bpag1 is included, termed plakins, comprises cytoskeleton binding proteins that are expressed as alternative splice forms (Fuchs and Karakesisoglou, 2001;Fuchs and Yang, 1999;Klymkowsky, 1999). To date, there have been at least five predominant isoforms of Bpag1 identified.…”

Section: Introductionmentioning

confidence: 99%

Bpag1 localization to actin filaments and to the nucleus is regulated by its N-terminus

Young

Pool

Kothary

2003

Journal of Cell Science

View full text Add to dashboard Cite

Plakins are a family of giant cytoskeleton binding proteins. One member of this group is bullous pemphigoid antigen 1 (Bpag1)/dystonin, which has neuronal and muscle isoforms that consist of actin-binding and microtubule-binding domains at either end separated by a plakin domain and several spectrin repeats. The better-characterized epithelial isoform has only the plakin domain in common with the neuronal and muscle isoforms. Here, we have analyzed the localization of muscle/neuronal (Bpag1a/b) isoforms and the epithelial (Bpag1e) isoform within C2C12 myoblast cells. Although an antibody specific to Bpag1a/b isoform 2 detected protein co-aligning actin stress fibers, this same antibody and two Bpag1e antibodies predominantly detected protein in the nuclei. A Bpag1a/b isoform 2 N-terminal fusion protein containing the plakin domain also localized to actin stress fibers and to nuclei.Within the plakin domain, we characterized a functional nuclear localization signal, which was responsible for localization of the fusion protein to the nucleus. Bpag1a/b isoform 1 N-terminal fusion proteins differed in their interaction with the actin cytoskeleton and with their ability to localize to the nucleus, suggesting that Bpag1 isoforms with different N-termini have differing roles. These results show the importance of N-terminal domains in dictating the localization and function of Bpag1 isoforms. We provide the first indication that Bpag1 is not strictly a cytoplasmic/membrane protein but that it can also localize to the nucleus.

show abstract

Bridging cytoskeletal intersections

Cited by 146 publications

References 91 publications

Nestin Promotes the Phosphorylation-dependent Disassembly of Vimentin Intermediate Filaments During Mitosis

Nestin Promotes the Phosphorylation-dependent Disassembly of Vimentin Intermediate Filaments During Mitosis

Primary cilia sensitize endothelial cells for fluid shear stress

Bpag1 localization to actin filaments and to the nucleus is regulated by its N-terminus

Contact Info

Product

Resources

About