Capturing protein tails by CAP-Gly domains
Cytoskeleton-associated protein-glycine-rich (CAP-Gly) domains are protein-interaction modules implicated in important cellular processes and in hereditary human diseases. A prominent function of CAP-Gly domains is to bind to C-terminal EEY/F-COO(-) sequence motifs present in alpha-tubulin and in some microtubule-associated protein tails; however, CAP ...
Steinmetz Michel O, Akhmanova Anna
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Mammalian CARMIL Inhibits Actin Filament Capping by Capping Protein [PDF]
Actin polymerization in cells occurs via filament elongation at the barbed end. Proteins that cap the barbed end terminate this elongation. Heterodimeric capping protein (CP) is an abundant and ubiquitous protein that caps the barbed end. We find that the mouse homolog of the adaptor protein CARMIL (mCARMIL) binds CP with high affinity and decreases ...
Yang, Changsong +6 more
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From filopodia to synapses: the role of actin‐capping and anti‐capping proteins [PDF]
AbstractActin‐capping and anti‐capping proteins are crucial regulators of actin dynamics. Recent studies have indicated that these proteins may be heavily involved in all stages of synaptogenesis, from the emergence of filopodia, through neuritogenesis and synaptic contact stabilization, to the structural changes occurring at the synapse during ...
E. Menna +3 more
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CAPS-1 and CAPS-2 Are Essential Synaptic Vesicle Priming Proteins [PDF]
Before transmitter-filled synaptic vesicles can fuse with the plasma membrane upon stimulation they have to be primed to fusion competence. The regulation of this priming process controls the strength and plasticity of synaptic transmission between neurons, which in turn determines many complex brain functions.
Jockusch, Wolf J. +6 more
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Purification of capping protein using the capping protein binding site of CARMIL as an affinity matrix [PDF]
Capping protein (CP) is a ubiquitously expressed, heterodimeric actin binding protein that is essential for normal actin dynamics in cells. The existing methods for purifying native CP from tissues and recombinant CP from bacteria are time-consuming processes that involve numerous conventional chromatographic steps and functional assays to achieve a ...
Kirsten, Remmert +2 more
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Formin Leaky Cap Allows Elongation in the Presence of Tight Capping Proteins [PDF]
Formins, characterized by formin homology domains FH1 and FH2, are required to assemble certain F-actin structures including actin cables, stress fibers, and the contractile ring. FH1FH2 in a recombinant fragment from a yeast formin (Bni1p) nucleates actin filaments in vitro. It also binds to the filament barbed end where it appears to act as a "leaky"
Zigmond, Sally H. +7 more
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Cap Z, a calcium insensitive capping protein in resting and activated platelets [PDF]
Capping of the barbed‐ends of actin filaments is an important mechanism for control of the cytoskeleton. In platelets, a valuable model system, it has been thought that gelsolin was the major capping protein. We now report that platelets contain 2 μM Cap Z, a calcium insensitive heterodimeric capping protein; two major and additional minor isoforms of ...
Nachmias, Vivianne T. +3 more
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Eotaxin and Capping Protein in Experimental Vasculopathy [PDF]
Ischemia-induced tissue activation may contribute to the pathogenesis of graft vasculopathy, but the mediators implicated have only partially been characterized. To gain further insight into the molecular mechanisms involved, syngeneic rat aortic transplants with cold-storage-induced vasculopathy were studied for differentially expressed mRNA ...
J, Chen +4 more
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CAP protein superfamily members in Toxocara canis. [PDF]
Proteins of the cysteine-rich secretory proteins, antigen 5 and pathogenesis-related 1 (CAP) superfamily are recognized or proposed to play roles in parasite development and reproduction, and in modulating host immune attack and infection processes. However, little is known about these proteins for most parasites.In the present study, we explored CAP ...
Stroehlein AJ +7 more
europepmc +4 more sources
Folding transitions during assembly of the eukaryotic mRNA cap-binding complex. [PDF]
The cap-binding protein eIF4E is the first in a chain of translation initiation factors that recruit 40S ribosomal subunits to the 5' end of eukaryotic mRNA. During cap-dependent translation, this protein binds to the 5'-terminal m(7)Gppp cap of the mRNA,
von der Haar, Tobias +8 more
core +1 more source

