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Actin Capping Protein

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John A. Cooper – One of the best experts on this subject based on the ideXlab platform.

  • comparative analysis of cpi motif regulation of biochemical functions of Actin Capping Protein
    Biochemistry, 2020
    Co-Authors: Patrick Mcconnell, Marlene Mekel, Alexander G Kozlov, Olivia L Mooren, Timothy M Lohman, John A. Cooper
    Abstract:

    The heterodimeric Actin Capping Protein (CP) is regulated by a set of Proteins that contain CP-interActing (CPI) motifs. Outside of the CPI motif, the sequences of these Proteins are unrelated and …

  • comparative analysis of cpi motif regulation of biochemical functions of Actin Capping Protein
    bioRxiv, 2020
    Co-Authors: Patrick Mcconnell, Marlene Mekel, Alexander G Kozlov, Olivia L Mooren, Timothy M Lohman, John A. Cooper
    Abstract:

    The heterodimeric Actin Capping Protein (CP) is regulated by a set of Proteins that contain CP-interActing (CPI) motifs. Outside of the CPI motif, the sequences of these Proteins are unrelated and distinct. The CPI motif and surrounding sequences are conserved within a given Protein family, when compared to those of other CPI-motif Protein families. Using biochemical assays with purified Proteins, we compared the ability of CPI-motif-containing peptides from different Protein families to a) bind to CP, b) allosterically inhibit barbed-end Capping by CP, and c) allosterically inhibit interaction of CP with V-1, another regulator of CP. We found large differences in potency among the different CPI-motif-containing peptides, and the different functional assays showed different orders of potency. These biochemical differences among the CPI-motif peptides presumably reflect interactions between CP and CPI-motif peptides involving amino-acid residues that are conserved but are not part of the strictly defined consensus, as it was originally identified in comparisons of sequences of CPI motifs(1, 2) across all Protein families (1, 2). These biochemical differences may be important for conserved distinct functions of CPI-motif Protein families in cells with respect to the regulation of CP activity and Actin assembly near membranes.

  • mechanism for carmil Protein inhibition of heterodimeric Actin Capping Protein
    Journal of Biological Chemistry, 2012
    Co-Authors: Taekyung Kim, David Sept, Geoffrey E Ravilious, John A. Cooper
    Abstract:

    Capping Protein (CP) controls the polymerization of Actin filaments by Capping their barbed ends. In lamellipodia, CP dissociates from the Actin cytoskeleton rapidly, suggesting the possible existence of an unCapping factor, for which the Protein CARMIL (Capping Protein, Arp2/3 and myosin-I linker) is a candidate. CARMIL binds to CP via two motifs. One, the CP interaction (CPI) motif, is found in a number of unrelated Proteins; the other motif is unique to CARMILs, the CARMIL-specific interaction motif. A 115-aa CARMIL fragment of CARMIL with both motifs, termed the CP-binding region (CBR), binds to CP with high affinity, inhibits Capping, and causes unCapping. We wanted to understand the structural basis for this function. We used a collection of mutants affecting the Actin-binding surface of CP to test the possibility of a steric-blocking model, which remained open because a region of CBR was not resolved in the CBR/CP co-crystal structure. The CP Actin-binding mutants bound CBR normally. In addition, a CBR mutant with all residues of the unresolved region changed showed nearly normal binding to CP. Having ruled out a steric blocking model, we tested an allosteric model with molecular dynamics. We found that CBR binding induces changes in the conformation of the Actin-binding surface of CP. In addition, ∼30-aa truncations on the Actin-binding surface of CP decreased the affinity of CBR for CP. Thus, CARMIL promotes unCapping by binding to a freely accessible site on CP bound to a filament barbed end and inducing a change in the conformation of the Actin-binding surface of CP.

Jeffrey S. Simske – One of the best experts on this subject based on the ideXlab platform.

Sofia Khaitlina – One of the best experts on this subject based on the ideXlab platform.

Maki K. Yamada – One of the best experts on this subject based on the ideXlab platform.

  • Activity‐dependent localization in spines of the F‐Actin Capping Protein CapZ screened in a rat model of dementia
    Genes to cells : devoted to molecular & cellular mechanisms, 2010
    Co-Authors: Takuma Kitanishi, Jun Sakai, Shinichi Kojima, Yoshito Saitoh, Kaoru Inokuchi, Masahiro Fukaya, Masahiko Watanabe, Norio Matsuki, Maki K. Yamada
    Abstract:

    Actin reorganization in dendritic spines is hypothesized to underlie neuronal plasticity. Actin-related Proteins, therefore, might serve as useful markers of plastic changes in dendritic spines. Here, we utilized memory deficits induced by fimbria-fornix transection (FFT) in rats as a dementia model to screen candidate memory-associated molecules by using a two-dimensional gel method. Comparison of Protein profiles between the transected and control sides of hippocampi after unilateral FFT revealed a reduction in the F-Actin Capping Protein (CapZ) signal on the FFT side. Subsequent immunostaining of brain sections and cultured hippocampal neurons revealed that CapZ localized in dendritic spines and the signal intensity in each spine varied widely. The CapZ content decreased after suppression of neuronal firing by tetrodotoxin treatment in cultured neurons, indicating rapid and activity-dependent regulation of CapZ accumulation in spines. To test input specificity of CapZ accumulation in vivo, we delivered high-frequency stimuli to the medial perforant path unilaterally in awake rats. This path selectively inputs to the middle molecular layer of the dentate gyrus, where CapZ immunoreactivity increased. We conclude that activity-dependent, synapse-specific regulation of CapZ redistribution might be important in both maintenance and remodeling of synaptic connections in neurons receiving specific spatial and temporal patterns of inputs.

  • activity dependent localization in spines of the f Actin Capping Protein capz screened in a rat model of dementia
    Genes to Cells, 2010
    Co-Authors: Takuma Kitanishi, Maki K. Yamada, Jun Sakai, Shinichi Kojima, Yoshito Saitoh, Kaoru Inokuchi, Masahiro Fukaya, Masahiko Watanabe, Norio Matsuki
    Abstract:

    Actin reorganization in dendritic spines is hypothesized to underlie neuronal plasticity. Actin-related Proteins, therefore, might serve as useful markers of plastic changes in dendritic spines. Here, we utilized memory deficits induced by fimbria-fornix transection (FFT) in rats as a dementia model to screen candidate memory-associated molecules by using a two-dimensional gel method. Comparison of Protein profiles between the transected and control sides of hippocampi after unilateral FFT revealed a reduction in the F-Actin Capping Protein (CapZ) signal on the FFT side. Subsequent immunostaining of brain sections and cultured hippocampal neurons revealed that CapZ localized in dendritic spines and the signal intensity in each spine varied widely. The CapZ content decreased after suppression of neuronal firing by tetrodotoxin treatment in cultured neurons, indicating rapid and activity-dependent regulation of CapZ accumulation in spines. To test input specificity of CapZ accumulation in vivo, we delivered high-frequency stimuli to the medial perforant path unilaterally in awake rats. This path selectively inputs to the middle molecular layer of the dentate gyrus, where CapZ immunoreactivity increased. We conclude that activity-dependent, synapse-specific regulation of CapZ redistribution might be important in both maintenance and remodeling of synaptic connections in neurons receiving specific spatial and temporal patterns of inputs.

Andrés F Muro – One of the best experts on this subject based on the ideXlab platform.