Membrane/Cytoskeleton Communication

Meiri, Karina F.

doi:10.1007/978-1-4757-5806-1_8

Cited by 24 publications

(13 citation statements)

References 162 publications

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“…Many cytoskeletal proteins are known to be specifically enriched in rafts either directly by insertion into the lipid bilayer, or indirectly via interactions with other raft components [71,72] where they can modulate cytoskeletal dynamics directly [73,74]. This is in agreement with the observation that platelet lipid rafts specifically associated with the actin cytoskeleton in an IIb 3 -dependent manner, thereby playing an important role in the organization of the membrane-cytoskeleton linkage [70].…”

Section: Proteomic Profiling Of Platelet Lipid Raftssupporting

confidence: 78%

Recent Advances in the Characterisation of the Platelet Membrane System by Proteomics

Foy

Maguire²

2007

CPD

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Platelets are the principle effectors of cellular haemostasis and key mediators in the pathogenesis of thrombosis. A variety of membrane receptors determine platelet reactivity with numerous agonists and adhesive proteins, and therefore represent key targets for the development of antiplatelet drug therapy. Here, we summarise recent advances in the analysis of the complex platelet membrane system achieved through the integration of platelet biology and proteomics.

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Section: Proteomic Profiling Of Platelet Lipid Raftssupporting

confidence: 78%

Recent Advances in the Characterisation of the Platelet Membrane System by Proteomics

Foy

Maguire²

2007

CPD

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“…The actin filament-associated protein, GAP43, known for its role in F-actin stabilization and synaptic changes, showed increased phosphorylation after 6 hr of SD. Phosphorylation at Ser 41 by protein kinase C occurs in response to extracellular signals and stabilizes actin filaments by removing them from the polymerization-depolymerization cycle (Meiri, 2004). Yet another protein involved in cytoskeletal remodeling and membrane trafficking, RhoA GTPase, increased during SD.…”

Section: Discussionmentioning

confidence: 99%

Sleep deprivation‐induced protein changes in basal forebrain: Implications for synaptic plasticity

Basheer

Brown

Ramesh

et al. 2005

J of Neuroscience Research

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The need to sleep is universal and lack of sleep often results in decreases in alertness and cognitive function. Data suggest that sleep-related mechanisms and deficits resulting from loss of sleep are associated anatomically with the basal forebrain. Long-term effects of sleep deprivation, those lasting a day or more, likely require transcriptional changes leading to changes in protein synthesis, whereas short-term effects may be mediated by rapid changes in the functional status of proteins. To understand sleep deprivation-induced changes in proteins in the wake-promoting area of the basal forebrain in rat, proteomic analysis was carried out by a combination of 2D gel electrophoresis to separate and visualize proteins and matrix-assisted laser desorption/ionization time-of flight mass spectrometry for protein identification. Among 969 protein spots that were compared, 89 spots showed more than a twofold difference between 6-hr sleep-deprived rats and undisturbed sleeping controls. We have identified 11 of these proteins to be either cytoskeletal or associated with synapses. The changes in four of these proteins were analyzed further by Western blots of 1D and 2D. Two proteins associated with the cytoskeleton, tubulin and GAP43, show posttranslational modifications. Increased tyrosination of alpha tubulin isoforms and increased phosphorylation of GAP43 was observed after 6-hr sleep deprivation when compared to that in sleeping controls. The synaptic protein synaptosomal-associated protein-25 (SNAP25) is decreased whereas amphiphysin is phosphorylated after sleep deprivation. These changes in proteins in the basal forebrain during short-term sleep deprivation are suggestive of changes in the substrate for neuronal transmission and plasticity.

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“…The actin filaments (or F-actin) and the associated signaling machinery control many aspects of cell motility and provide the kinetic force that moves T cells (Samstag et al, 2003; Smith et al, 2007; Long et al, 2004; Pribila and Shimizu, 2003; Hogg et al, 2004); these systems also control the morphology and plasticity of T cells (Cogoli-Greuter et al, 2004; Dustin et al, 2004; Dustin, 2007; Krummel and Macara, 2006; Meiri, 2004; Miyamoto et al, 2003; Poenie et al, 2004; Pribila and Shimizu, 2003). The microtubule system is thought to regulate the polarized secretion of effector molecules and might contribute to receptor endocytosis as well as to the maintenance of F-actin dependent structures (Rey et al, 2007; Stradal et al, 2006; Bossi and Griffiths, 2005; Huse et al, 2008; Song et al, 2008; Gomez and Billadeau, 2008).…”

Section: Introductionmentioning

confidence: 99%

Age-related defects in the cytoskeleton signaling pathways of CD4 T cells

Garcia¹,

Miller²

2011

Ageing Research Reviews

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SummaryIt has been postulated that the cytoskeleton controls many aspects of T cell function, including activation, proliferation and apoptosis. Recent advances in our understanding of F-actin polymerization and the Ezrin-Radixin-Moesin (ERM) family of cytoskeleton signal proteins have provided new insights into immunological synapse formation during T cell activation. During aging there is a significant decline of T cell function largely attributable to declines in activation of CD4 T cells and defects in the formation of the immunological synapse. Here we discuss recent progress in the understanding of how aging alters F-actin and ERM proteins in mouse CD4 T cells, and the implications of these changes for the T cell activation process.

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Membrane/Cytoskeleton Communication

Cited by 24 publications

References 162 publications

Recent Advances in the Characterisation of the Platelet Membrane System by Proteomics

Recent Advances in the Characterisation of the Platelet Membrane System by Proteomics

Sleep deprivation‐induced protein changes in basal forebrain: Implications for synaptic plasticity

Age-related defects in the cytoskeleton signaling pathways of CD4 T cells

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