HSPB1, actin filament dynamics, and aging cells

Doshi, Bindi M.; Hightower, Lawrence E.; Lee, Juliet

doi:10.1111/j.1749-6632.2010.05191.x

Cited by 47 publications

(45 citation statements)

References 55 publications

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“…HspB1, that is Heat shock protein beta-1, also donated Hsp25 (mouse) and Hsp27 (human), is the most widely distributed and well studied sHsp (Ferns et al, 2006). Thus it may play a vital role in maintaining normal protein structure, and cell response to stress tolerance (Doshi et al, 2010). High expressed HspB1 play a vital role in promoting neuronal survival and regeneration following peripheral nerve injury, survival of injured sensory and motor neurons (Carmichael et al, 2002; O'Reilly et al, 2010).…”

Section: Discussionmentioning

confidence: 99%

Comparative Proteomics Analysis of Colorectal Cancer

Wang¹,

Liu²,

Zheng³

et al. 2012

Asian Pacific Journal of Cancer Prevention

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Background and Objective: Protein expression in colon and rectal cancer (CRC) and paired normal tissues was examined by two-dimensional gel electrophoresis (2-DE) to identify differentially expressed proteins. Materials and Methods: Five fresh colorectal cancer and paired adjacent normal tissues were obtained and differentially expressed protein spots were determined using PDQuest software, with identification on the basis of MALDI-TOF mass spectra. Results: Compared with normal colorectal mucosa, protein abnormal expression of 65 spots varying more than 1.5 times were found in 2-DE gels from colorectal cancer samples (P<0.05); forty-two proteins were up-regulated and 23 were down-regulated; twelve protein spots were identified using mass spectrometry, of which 8 were up-regulated, includimng HSPB1and Annexin A4, while 4 were down-regulated, the results being consistent with Western blot findings. Conclusions: Two-dimensional electrophoresis reference maps for CRC tissues and adjacent normal mucosa (NMC) were established and 12 differentially expressed proteins were identified. Up-regulated HSPB1 and Annexin A4 may play many important roles in the pathogenesis of colorectal cancer. cancer. In this study, the differentially expressed proteins between CRC and normal tissues were identified and differential protein expression profiles were established by proteomic approach, which provides a theoretical basis and foundation for further searching for the potential biomarkers and therapeutic targets relevant to human CRC occurrence and development.

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Section: Discussionmentioning

confidence: 99%

Comparative Proteomics Analysis of Colorectal Cancer

Wang¹,

Liu²,

Zheng³

et al. 2012

Asian Pacific Journal of Cancer Prevention

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“…The abundance of HSP27 modulates the actin cytoskeleton and influences cell migration (Mounier and Arrigo 2002;Salinthone et al 2008;Doshi et al 2010). In vitro, HSP27 was proposed to sequester actin monomers and weakly cap F-actin in a phosphorylation-dependent manner During et al 2007;Doshi et al 2010;Jia et al 2010).…”

Section: Igf2bp1 Controls Actin Dynamics By Antagonizing the Phosphormentioning

confidence: 99%

“…MAPK4 activates MK5 by phosphorylating the latter at T182, resulting in cytoplasmic accumulation of MK5 (Kant et al 2006;Coulombe and Meloche 2007;Deleris et al 2008;Perander et al 2008;Aberg et al 2009). MK5, in turn, phosphorylates HSP27 (HSPB1) and was suggested to thereby induce altered microfilament organization Doshi et al 2010). PTEN interferes with PIP 3 -directed activation of various signaling molecules, including small GTPases like RAC1 or protein kinases of the AKT family.…”

Section: Igf2bp1 Antagonizes the Phosphorylation Of Hsp27 By Interfermentioning

confidence: 99%

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IGF2BP1 promotes cell migration by regulating MK5 and PTEN signaling

et al. 2012

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In primary neurons, the oncofetal RNA-binding protein IGF2BP1 (IGF2 mRNA-binding protein 1) controls spatially restricted b-actin (ACTB) mRNA translation and modulates growth cone guidance. In cultured tumorderived cells, IGF2BP1 was shown to regulate the formation of lamellipodia and invadopodia. However, how and via which target mRNAs IGF2BP1 controls the motility of tumor-derived cells has remained elusive. In this study, we reveal that IGF2BP1 promotes the velocity and directionality of tumor-derived cell migration by determining the cytoplasmic fate of two novel target mRNAs: MAPK4 and PTEN. Inhibition of MAPK4 mRNA translation by IGF2BP1 antagonizes MK5 activation and prevents phosphorylation of HSP27, which sequesters actin monomers available for F-actin polymerization. Consequently, HSP27-ACTB association is reduced, mobilizing cellular G-actin for polymerization in order to promote the velocity of cell migration. At the same time, stabilization of the PTEN mRNA by IGF2BP1 enhances PTEN expression and antagonizes PIP 3 -directed signaling. This enforces the directionality of cell migration in a RAC1-dependent manner by preventing additional lamellipodia from forming and sustaining cell polarization intrinsically. IGF2BP1 thus promotes the velocity and persistence of tumor cell migration by controlling the expression of signaling proteins. This fine-tunes and connects intracellular signaling networks in order to enhance actin dynamics and cell polarization.

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“…4A and supplemental Table S9). For example, heat shock protein 90 ␤ (HSP90AB1; clusters 1 and 3), heat shock protein 105 kDa (HSPH1; cluster 1), and histone acetyltransferase p300 (EP300; cluster 3) are required for the chaperon complex function (52)(53)(54). On the other hand, lamin-B1 (LMNB1; cluster 1 and 2), inner nuclear membrane protein Man1 (LEMD3; cluster 1 and 3), and lamina-associated polypeptide 2 (TMPO; cluster 1 and 3) are important regulators during the development of intermediate filaments (55)(56)(57).…”

Section: Temporal Clustering and Mathematical Modeling Reveal A Respomentioning

confidence: 99%

Temporal Phosphoproteome Dynamics Induced by an ATP Synthase Inhibitor Citreoviridin*

Hsu

Wang³

et al. 2015

Molecular & Cellular Proteomics

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Citreoviridin, one of toxic mycotoxins derived from fungal species, can suppress lung cancer cell growth by inhibiting the activity of ectopic ATP synthase, but has limited effect on normal cells. However, the mechanism of citreoviridin triggering dynamic molecular responses in cancer cells remains unclear. Here, we performed temporal phosphoproteomics to elucidate the dynamic changes after citreoviridin treatment in cells and xenograft model. We identified a total of 829 phosphoproteins and demonstrated that citreoviridin treatment affects protein folding, cell cycle, and cytoskeleton function. Furthermore, response network constructed by mathematical modeling shows the relationship between the phosphorylated heat shock protein 90 β and mitogen-activated protein kinase signaling pathway. This work describes that citreoviridin suppresses cancer cell growth and mitogenactivated protein kinase/extracellular signal-regulated kinase signaling by site-specific dephosphorylation of HSP90AB1 on Serine 255 and provides perspectives in cancer therapeutic strategies. Molecular & Cellular

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HSPB1, actin filament dynamics, and aging cells

Cited by 47 publications

References 55 publications

Comparative Proteomics Analysis of Colorectal Cancer

Comparative Proteomics Analysis of Colorectal Cancer

IGF2BP1 promotes cell migration by regulating MK5 and PTEN signaling

Temporal Phosphoproteome Dynamics Induced by an ATP Synthase Inhibitor Citreoviridin*

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