A5088598466- Cellular Mechanics and Interactions
- Alzheimer's disease research and treatments
- Advanced Fluorescence Microscopy Techniques
- Cardiomyopathy and Myosin Studies
- Axon Guidance and Neuronal Signaling
- Cellular transport and secretion
- Cell Adhesion Molecules Research
- Microtubule and mitosis dynamics
- Neuroscience and Neuropharmacology Research
- Cell Image Analysis Techniques
- S100 Proteins and Annexins
- Nerve injury and regeneration
- RNA Research and Splicing
- Neuroinflammation and Neurodegeneration Mechanisms
- Mycotoxins in Agriculture and Food
- Nuclear Structure and Function
- Muscle Physiology and Disorders
- Prion Diseases and Protein Misfolding
- Viral Infectious Diseases and Gene Expression in Insects
- Force Microscopy Techniques and Applications
- Molecular Biology Techniques and Applications
- Mitochondrial Function and Pathology
- Biotin and Related Studies
- Neurobiology and Insect Physiology Research
- Advanced Proteomics Techniques and Applications
Colorado State University
2014-2024
Collins College
1989-2014
University of California, San Francisco
1997-2009
University of Minnesota System
2009
University of Geneva
2005
Florida College
2005
University of Florida
2005
University of Pennsylvania
1999
Chiba University
1996-1997
University of Otago
1996
Actin depolymerizing factor (ADF) occurs naturally in two forms, one of which contains a phosphorylated Ser and does not bind G-actin or depolymerize F-actin. Removal this phosphate vitro by alkaline phosphatase restores full F-actin activity. To identify the phosphorylation site, [32P]pADF was purified digested with endoproteinase Lys-C. The digest contained only 32P-labeled peptide. Further digestion Asp-N mass spectrometric analysis showed that peptide came from N terminus ADF. Alkaline...
In cultured chick ciliary neurons, when ATP synthesis is inhibited, depletion reduced ∼50% by slowing actin filament turnover with jasplakinolide or latrunculin A. Jasplakinolide inhibits disassembly, and A prevents assembly sequestering monomers. Cytochalasin D, which allows assembly–disassembly, but only at pointed ends, less effective in conserving ATP. Ouabain, an Na<sup>+</sup>–K<sup>+</sup>-ATPase inhibitor, both prevent of the loss. When applied together, they completely loss over a...
Abstract Brain or muscle F‐actin is rapidly depolymerized to monomeric actin in vitro by actin‐depolymerizing factor, a protein isolated from chick embryo brain. Binding of tropomyosin protects the depolymerization this factor. A 8.4/1.0 molar ratio subunits tropomyosin, achieved incubation with excess 58% factor for at least 3 hr 25°C. Thus, seems be specifically directed toward filaments lacking tropomyosin.
The actin assembly-regulating activity of depolymerizing factor (ADF)/ cofilin is inhibited by phosphorylation. Studies were undertaken to characterize the signaling pathways and phosphatases involved in activating phosphorylated ADF (pADF), emphasizing signals related neuronal process extension. Western blots using antibodies cofilin, as well an ADF/cofilin phosphoepitope-specific antibody characterized this paper, used measure changes phosphorylation state phosphate turnover response...
The establishment of polarity is an essential process in early neuronal development. Although a number molecules controlling have been identified, genetic evidence about their physiological roles this mostly lacking. We analyzed the consequences loss Cdc42, central regulator multiple systems, on polarization mammalian neurons. Genetic ablation Cdc42 brain led to abnormalities, including striking defects formation axonal tracts. Neurons from null animals sprouted neurites but had strongly...
The specific functions of greater than 40 vertebrate nonmuscle tropomyosins (Tms) are poorly understood. In this article we have tested the ability two Tm isoforms, TmBr3 and human homologue Tm5 (hTM5 NM1 ), to regulate actin filament function. We found that these Tms can differentially alter organization, cell size, shape. hTm5 was able recruit myosin II into stress fibers, which resulted in decreased lamellipodia cellular migration. contrast, transfection induced lamellipodial formation,...
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTAnalysis of the interactions actin depolymerizing factor with G- and F-actinS. M. Hayden, P. S. Miller, A. Brauweiler, J. R. BamburgCite this: Biochemistry 1993, 32, 38, 9994–10004Publication Date (Print):September 28, 1993Publication History Published online1 May 2002Published inissue 28 September 1993https://pubs.acs.org/doi/10.1021/bi00089a015https://doi.org/10.1021/bi00089a015research-articleACS PublicationsRequest reuse permissionsArticle...
In contrast to the slow rate of depolymerization pure actin in vitro, populations filaments vivo turn over rapidly. Therefore, must be accelerated by one or more factors cell. Since dynamics Listeria monocytogenes tails bear many similarities those lamellipodia moving cells, we have used as a model system isolate required for regulating rapid filament turnover involved cell migration. Using cell-free Xenopus egg extract reproduce movement seen cell, depleted candidate depolymerizing proteins...
Two cDNAs, isolated from a Xenopus laevis embryonic library, encode proteins of 168 amino acids, both which are 77% identical to chick cofilin and 66% actin-depolymerizing factor (ADF), two structurally functionally related proteins. These ADF/cofilins (XADs) differ each other in 12 residues spread throughout the sequence but do not charge. Purified GST-fusion have pH-dependent F-actin-binding activities similar ADF cofilin. Similarities developmental tissue specific expression,...
Actin depolymerizing factor (ADF) is a low molecular mass (19 kD) protein that forms tightly bound dimeric complex with actin. We have raised rabbit antiserum to chick brain ADF and used it analyze the distribution cellular localization of ADF. find major constituent all embryonic most adult tissues examined, accounting for 0.1-0.4% total protein. Some as much 0.6 mol per mole Adult heart skeletal muscle are unusual in having very levels ADF: less than 0.02% soluble During development...