Small Heat Shock Protein 27 (HSP27) Associates with Tubulin/Microtubules in HeLa Cells

Hino, Mizuki; Kurogi, Kazuki; Okubo, Masa Aki; Murata‐Hori, Maki; Hosoya, Hiroshi

doi:10.1006/bbrc.2000.2553

Cited by 96 publications

(64 citation statements)

References 25 publications

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“…2). However, we detected the majority of HSP27 in a MT-enriched fraction of pulmonary artery EC (139), and interaction between tubulin/MT and HSP27 in other cell types has also been reported (63), raising the question of whether HSP27 is a link between MT and microfilaments in agonistevoked responses. On the other hand, tau is directly related to MT; its unphosphorylated form supports MT assembly and inhibits the rate of depolymerization (36).…”

Section: Pp2a and Cytoskeletonmentioning

confidence: 66%

Regulation of vascular endothelial cell barrier function and cytoskeleton structure by protein phosphatases of the PPP family

Csortos¹,

Kolosova²,

Verin³

2007

American Journal of Physiology-Lung Cellular and Molecular Phys

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Section: Pp2a and Cytoskeletonmentioning

confidence: 66%

Regulation of vascular endothelial cell barrier function and cytoskeleton structure by protein phosphatases of the PPP family

Csortos¹,

Kolosova²,

Verin³

2007

American Journal of Physiology-Lung Cellular and Molecular Phys

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“…44 Furthermore, hsp27 has been shown to associate with microtubules. 45 The overexpression of multiple genes associated with microtubule function and possibly centrosome regulation raises the possibility that a possible locus of deregulation in early stages of rat mammary gland carcinogenesis involves defects in the function of the mitotic spindle that could potentially lead to chromosomal segregation abnormalities and aneuploidy.…”

Section: Discussionmentioning

confidence: 99%

Gene expression profiling in the mammary gland of rats treated with 7,12‐dimethylbenz[a]anthracene

Papaconstantinou

Shanmugam

Shan

et al. 2005

Intl Journal of Cancer

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Identification of molecular markers of early‐stage breast cancer development is important for the diagnosis and prevention of the disease. In the present study, we used microarray analysis to examine the differential expression of genes in the rat mammary gland soon after treatment with a known chemical carcinogen, 7,12‐dimethylbenz[a]anthracene (DMBA), and prior to tumor development. Six weeks after DMBA, differential expression of multiple genes involved in cell growth, differentiation and microtubule dynamics were observed. Gene expression changes were further validated by a combination of techniques, including real‐time PCR, RT‐PCR, Western blotting and immunohistochemistry. An inhibition of differentiation in this early stage was suggested by the lower expression of β‐casein and transferrin and higher expression of hsp27 in glands from DMBA‐treated rats. Possible cell cycle deregulation was indicated by an increased expression of cyclin D1 and hsp86, a heat shock protein associated with cyclin D1. Prior to tumor development, DMBA increased cellular proliferation as detected by Ki‐67 and stathmin immunostaining in histologically normal mammary gland. Genes regulating microtubule function, including stathmin, Ran, α‐tubulin and hsp27, were all overexpressed in the mammary gland of DMBA‐treated rats, raising the possibility that disruption of microtubule dynamics and abnormal mitosis may be critical events preceding breast cancer development. Several of the altered proteins, including hsp27, hsp86 and stathmin, may ultimately serve as markers of early breast cancer development. Published 2005 Wiley‐Liss, Inc.

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“…HeLa Rho-kinase was immunoprecipitated with anti-Rhokinase antibody as described previously (Hino et al, 2000). HeLa cell extracts in Triton/glycerol solution were centrifuged at 100 000 g for 2 h in order to precipitate actin cytoskeleton.…”

Section: Phosphorylation Assay Of Immunopurified Rho-kinase In Vitromentioning

confidence: 99%

Rho-kinase contributes to diphosphorylation of myosin II regulatory light chain in nonmuscle cells

et al. 2002

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Phosphorylation of myosin II regulatory light chain (MRLC) is important for cell motility and cytokinesis in nonmuscle cells. Although the regulation of monophosphorylated MRLC at serine 19 throughout the cell cycle was examined in detail, MRLC diphosphorylation at both threonine 18 and serine 19 is still unclear. Here we found that Rho-kinase has an activity for MRLC diphosphorylation in nonmuscle cells using sequential column chromatographies. Transfection of Rho-kinase-EGFP induced the excess diphosphorylated MRLC and the bundling of the actin filaments. Conversely, the treatment of cells with a specific inhibitor of Rho-kinase, Y-27632, resulted in the decrease of endogenous diphosphorylated MRLC and actin stress fibers. Immunolocalization studies showed that both diphosphorylated MRLC and Rho-kinase accumulated and colocalized at the contractile ring and the midbody in dividing cells. Taken together, it is suggested that Rho-kinase contributes to MRLC diphosphorylation and reorganization of actin filaments in nonmuscle cells.

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Small Heat Shock Protein 27 (HSP27) Associates with Tubulin/Microtubules in HeLa Cells

Cited by 96 publications

References 25 publications

Regulation of vascular endothelial cell barrier function and cytoskeleton structure by protein phosphatases of the PPP family

Regulation of vascular endothelial cell barrier function and cytoskeleton structure by protein phosphatases of the PPP family

Gene expression profiling in the mammary gland of rats treated with 7,12‐dimethylbenz[a]anthracene

Rho-kinase contributes to diphosphorylation of myosin II regulatory light chain in nonmuscle cells

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