Stathmin interaction with HSC70 family proteins

Manceau, Valérie; Gavet, Olivier; Curmi, Patrick A.; Sobel, André

doi:10.1002/(sici)1522-2683(19990201)20:2<409::aid-elps409>3.0.co;2-n

Cited by 21 publications

(8 citation statements)

References 69 publications

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“…However, if that change has any direct relationship with the STMN1 is not known. Apart from its interaction with the microtubule system, STMN1 has been shown to interact with heat shock protein 70 (HSP70) proteins, particularly with heat shock cognate 70 (HSC70) (Manceau et al, 1999). In line with that, we have also identified significant changes in the expression of HSP70 proteins, including HSC70.…”

Section: Alterations In the Proteins Associated With The Cytoskeletonsupporting

confidence: 82%

Analyses of the spleen proteome of chickens infected with Marek's disease virus

et al. 2009

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Marek's disease virus (MDV), which causes a lymphoproliferative disease in chickens, is known to induce host responses leading to protection against disease in a manner dependent on genetic background of chickens and virulence of the virus. In the present study, changes in the spleen proteome at 7, 14 and 21 days post-infection in response to MDV infection were studied using two-dimensional polyacrylamide gel electrophoresis. Differentially expressed proteins were identified using one-dimensional liquid chromatography electrospray ionization tandem mass spectrometry (1D LC ESI MS/MS). Comparative analysis of multiple gels revealed that the majority of changes had occurred at early stages of the disease. In total, 61 protein spots representing 48 host proteins were detected as either quantitatively (false discovery rate (FDR)or=2) or qualitatively differentially expressed at least once during different sampling points. Overall, the proteins identified in the present study are involved in a variety of cellular processes such as the antigen processing and presentation, ubiquitin-proteasome protein degradation (UPP), formation of the cytoskeleton, cellular metabolism, signal transduction and regulation of translation. Notably, early stages of the disease were characterized by changes in the UPP, and antigen presentation. Furthermore, changes indicative of active cell proliferation as well as apoptosis together with significant changes in cytoskeletal components that were observed throughout the experimental period suggested the complexity of the pathogenesis. The present findings provide a basis for further studies aimed at elucidation of the role of these proteins in MDV interactions with its host.

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Section: Alterations In the Proteins Associated With The Cytoskeletonsupporting

confidence: 82%

Analyses of the spleen proteome of chickens infected with Marek's disease virus

et al. 2009

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“…Hsc70 and tubulin both associate with stathmin, which is increased in the hippocampus in AD. Dephosphorylated stathmin sequesters tubulin to depolymerise microtubules, while in the phosphorylated state it associates with Hsc70 [18], providing further evidence that the proteins identified in this study are affected in the pathogenesis of AD.…”

Section: Protein Identifications and Biological Significancesupporting

confidence: 67%

Comparative proteomic analysis using samples obtained with laser microdissection and saturation dye labelling

Wilson

Marouga²,

Prime³

et al. 2005

Proteomics

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Comparative proteomic methods are rapidly being applied to many different biological systems including complex tissues. One pitfall of these methods is that in some cases, such as oncology and neuroscience, tissue complexity requires isolation of specific cell types and sample is limited. Laser microdissection (LMD) is commonly used for obtaining such samples for proteomic studies. We have combined LMD with sensitive thiol-reactive saturation dye labelling of protein samples and 2-D DIGE to identify protein changes in a test system, the isolated CA1 pyramidal neurone layer of a transgenic (Tg) rat carrying a human amyloid precursor protein transgene. Saturation dye labelling proved to be extremely sensitive with a spot map of over 5,000 proteins being readily produced from 5 mug total protein, with over 100 proteins being significantly altered at p < 0.0005. Of the proteins identified, all showed coherent changes associated with transgene expression. It was, however, difficult to identify significantly different proteins using PMF and MALDI-TOF on gels containing less than 500 mug total protein. The use of saturation dye labelling of limiting samples will therefore require the use of highly sensitive MS techniques to identify the significantly altered proteins isolated using methods such as LMD.

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“…In addition to the interaction with tubulin, the yeast two-hybrid as well as biochemical approaches isolated several molecules that interact with stathmin or SCG10. Sobel and colleagues have identified a putative RNA binding kinase termed KIS (Maucuer et al, 1995) and members of the heat shock protein family Hsp70 (Maucuer et al, 1995;Manceau et al, 1999) as stathmin-interacting proteins. How these proteins regulate stathmin function is not known yet.…”

Section: Scg10 and Stathmin Protein Interactionsmentioning

confidence: 99%

Role of the microtubule destabilizing proteins SCG10 and stathmin in neuronal growth

et al. 2003

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The related proteins SCG10 and stathmin are highly expressed in the developing nervous system. Recently it was discovered that they are potent microtubule destabilizing factors. While stathmin is expressed in a variety of cell types and shows a cytosolic distribution, SCG10 is neuron-specific and membrane-associated. It contains an N-terminal targeting sequence that mediates its transport to the growing tips of axons and dendrites. SCG10 accumulates in the central domain of the growth cone, a region that also contains highly dynamic microtubules. These dynamic microtubules are known to be important for growth cone advance and responses to guidance cues. Because overexpression of SCG10 strongly enhances neurite outgrowth, SCG10 appears to be an important factor for the dynamic assembly and disassembly of growth cone microtubules during axonal elongation. Phosphorylation negatively regulates the microtubule destabilizing activity of SCG10 and stathmin, suggesting that these proteins may link extracellular signals to the rearrangement of the neuronal cytoskeleton. A role for these proteins in axonal elongation is also supported by their growth-associated expression pattern in nervous system development as well as during neuronal regeneration.

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Stathmin interaction with HSC70 family proteins

Cited by 21 publications

References 69 publications

Analyses of the spleen proteome of chickens infected with Marek's disease virus

Analyses of the spleen proteome of chickens infected with Marek's disease virus

Comparative proteomic analysis using samples obtained with laser microdissection and saturation dye labelling

Role of the microtubule destabilizing proteins SCG10 and stathmin in neuronal growth

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