Local actin filament formation powers the development of the signal-receiving arbor of neurons that underlies neuronal network formation. Yet, little is known about the molecules that drive these processes and may functionally connect them to the transient calcium pulses observed in restricted areas in the forming dendritic arbor. Here we demonstrate that Cordon-Bleu (Cobl)-like, an uncharacterized protein suggested to represent a very distantly related, evolutionary ancestor of the actin nucleator Cobl, despite having only a single G-actin-binding Wiskott-Aldrich syndrome protein Homology 2 (WH2) domain, massively promoted the formation of F-actin-rich membrane ruffles of COS-7 cells and of dendritic branches of neurons. Cobl-like hereby integrates WH2 domain functions with those of the F-actin-binding protein Abp1. Cobl-like-mediated dendritic branching is dependent on Abp1 as well as on Ca/calmodulin (CaM) signaling and CaM association. Calcium signaling leads to a promotion of complex formation with Cobl-like's cofactor Abp1. Thus, Ca/CaM control of actin dynamics seems to be a much more broadly used principle in cell biology than previously thought.
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http://dx.doi.org/10.1083/jcb.201704071 | DOI Listing |
Cell Mol Life Sci
December 2024
Rudbeck Laboratory, Department of Immunology, Genetics and Pathology, Uppsala University, Uppsala, 75185, Sweden.
MTSS1 is a ubiquitously expressed intracellular protein known mainly for its involvement in basic cellular processes, such as the regulation of actin organization and membrane architecture. MTSS1 has attracted much attention for its role as a tumor suppressor, being absent or expressed at reduced levels in advanced and metastasizing cancers. Occasionally, MTSS1 is, instead, upregulated in metastasis and, in some cases, even in primary tumors.
View Article and Find Full Text PDFNature
August 2024
Department of Physiology and Biochemistry and Molecular Biophysics Graduate Group, University of Pennsylvania Perelman School of Medicine, Philadelphia, PA, USA.
Humans express 15 formins that play crucial roles in actin-based processes, including cytokinesis, cell motility and mechanotransduction. However, the lack of structures bound to the actin filament (F-actin) has been a major impediment to understanding formin function. Whereas formins are known for their ability to nucleate and elongate F-actin, some formins can additionally depolymerize, sever or bundle F-actin.
View Article and Find Full Text PDFJ Biol Chem
March 2024
HiLIFE Institute of Biotechnology, University of Helsinki, Helsinki, Finland; Faculty of Biological and Environmental Sciences, University of Helsinki, Helsinki, Finland. Electronic address:
Diseases caused by Leishmania and Trypanosoma parasites are a major health problem in tropical countries. Because of their complex life cycle involving both vertebrate and insect hosts, and >1 billion years of evolutionarily distance, the cell biology of trypanosomatid parasites exhibits pronounced differences to animal cells. For example, the actin cytoskeleton of trypanosomatids is divergent when compared with other eukaryotes.
View Article and Find Full Text PDFFood Chem
May 2024
College of Food Science and Technology, Agricultural University of Hebei, Hebei Agricultural Products Processing Technology Innovation Center, Baoding, Hebei 071000, China. Electronic address:
This study investigated proteomic changes in Penaeus vannamei in half-dried and dried shrimp using tandem mass-tag technology. After performing the drying treatment, the tandem mass-tag results revealed 1,162,306 spectra, 2997 quantifiable proteins, and 72 differentially expressed proteins (DEPs) compared with that in the untreated group. A total of 29 DEPs were found in the half-dried shrimp, while 49 DEPs were found in the dried shrimp.
View Article and Find Full Text PDFbioRxiv
December 2023
Departments of Physics, Cell biology and Biochemistry, Emory University, Atlanta, GA 30322, USA.
Cellular actin networks display distinct assembly and disassembly dynamics resulting from multicomponent reactions occurring primarily at the two ends and the sides of actin filaments [1-3]. While barbed ends are considered the hotspot of actin assembly [4], disassembly is thought to primarily occur via reactions on filament sides and pointed ends [3, 5-11]. Cyclase-associated protein (CAP) has emerged as the main protagonist of actin disassembly and remodeling - it collaborates with cofilin to increase pointed-end depolymerization by 300-fold [6, 7], promotes filament "coalescence" in presence of Abp1 [12], and accelerates nucleotide exchange to regenerate monomers for new rounds of assembly [13-15].
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