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Anita A Wasik, Surjya N Dash, Sanna Lehtonen
Septins are a conserved family of GTP-binding proteins that assemble into cytoskeletal filaments to function in a highly sophisticated and physiologically regulated manner. Originally septins were discovered in the budding yeast as membrane-associated filaments that affect cell polarity and cytokinesis. In the last decades, much progress has been made in understanding the biochemical properties and cell biological functions of septins. In line with this, mammalian septins have been shown to be involved in various cellular processes, including regulation of cell polarity, cytoskeletal organization, vesicle trafficking, ciliogenesis and cell-pathogen interactions...
July 13, 2018: Cytoskeleton
Bipan Kumar Deb, Gaiti Hasan
Orai channels are plasma membrane resident Ca2+ channels that allow extracellular Ca2+ uptake after depletion of ER-Ca2+ stores by a process called store-operated Ca2+ entry (SOCE). Septins of the SEPT2 subgroup act as positive regulators of SOCE in human non-excitable cells. SEPT2 subgroup septins form the central core of hetero-hexameric or hetero-octameric complexes with SEPT6, SEPT7 and SEPT9 subgroup septins. The presence of fewer septin encoding genes coupled with ease of genetic manipulation allows for better understanding of septin subgroup function in Drosophila...
July 13, 2018: Cytoskeleton
Joseph Marquardt, Xi Chen, Erfei Bi
The septin family of proteins have fascinated cell biologists for decades due to the elaborate architecture they adopt in different eukaryotic cells. Whether they exist as rings, collars, or gauzes in different cell types and at different times in the cell cycle illustrates a complex series of regulation in structure. While the organization of different septin structures at the cortex of different cell types during the cell cycle has been described to various degrees, the exact structure and regulation at the filament level is still largely unknown...
July 6, 2018: Cytoskeleton
Christopher J Alexander, Wolfgang Wagner, Neal G Copeland, Nancy A Jenkins, John A Hammer
The actin-based motor myosin Va transports numerous cargos, including the smooth endoplasmic reticulum (SER) in cerebellar Purkinje neurons (PNs) and melanosomes in melanocytes. Identifying proteins that interact with this myosin is key to understanding its cellular functions. Towards that end, we used recombineering to insert via homologous recombination a tandem affinity purification (TAP) tag composed of the IgG binding domain of Protein A, a TEV cleavage site, and a FLAG tag into the mouse MYO5A locus immediately after the initiation codon...
July 6, 2018: Cytoskeleton
Jushuo Wang, Yingli Fan, Jean M Sanger, Joseph W Sanger
De novo assembly of contractile myofibrils begins with the formation of premyofibrils where filaments of non-muscle myosin (NM II), and actin organize in sarcomeric patterns with Z-Bodies containing muscle-specific alpha-actinin. Interactions of muscle specific myosin (MM II) with NM II occur in a nascent myofibril stage that precedes the assembly of mature myofibrils. By the final stage of myofibrillogenesis, the only myosin II present in the mature myofibrils is MM II. In this current study of myofibril assembly, the three vertebrate isoforms of NM II (A, B, and C) and sarcomeric alpha-actinin, ligated to GFP family proteins, were coexpressed in avian embryonic skeletal and cardiac muscle cells...
May 21, 2018: Cytoskeleton
Camilla B Mitchell, Justine R Stehn, Geraldine M O'Neill
The migration and invasion of cells through tissues in the body is facilitated by a dynamic actin cytoskeleton. The actin-associating protein, tropomyosin Tpm3.1 has emerged to play important roles in cell migration and invasion. To date, investigations have focused on single cell migration and invasion where Tpm3.1 expression is inversely associated with Rac GTPase-mediated cell invasion. While single cell and collective cell invasion have many features in common, collective invasion is additionally impacted by cell-cell adhesion, and the role of Tpm3...
May 12, 2018: Cytoskeleton
Damián Lobato-Márquez, Sina Krokowski, Andrea Sirianni, Gerald Larrouy-Maumus, Serge Mostowy
Shigella flexneri, a Gram-negative enteroinvasive pathogen, causes inflammatory destruction of the human intestinal epithelium. During infection of epithelial cells, Shigella escape from the phagosome to the cytosol, where they reroute host cell glycolysis to obtain nutrients for proliferation. Septins, a poorly understood component of the cytoskeleton, can entrap cytosolic Shigella targeted to autophagy in cage-like structures to restrict bacterial proliferation. Although bacterial entrapment by septin caging has been the subject of intense investigation, the role of septins and the autophagy machinery in the proliferation of non-caged Shigella is mostly unknown...
May 12, 2018: Cytoskeleton
Megha Abbey, Matthias Gaestel, Manoj B Menon
Septins are conserved cytoskeletal proteins with unique filament forming capabilities and roles in cytokinesis and cell morphogenesis. Septins undergo hetero-oligomerization and assemble into higher order structures including filaments, rings and cages. Hetero- and homotypic interactions of septin isoforms involve alternating GTPase (G)-domain interfaces and those mediated by N- and C-terminal extensions. While most septins bind GTP, display weak GTP-hydrolysis activity and incorporate guanine nucleotides in their interaction interfaces, studies using GTPase-inactivating mutations have failed to conclusively establish a crucial role for GTPase activity in mediating septin functions...
May 10, 2018: Cytoskeleton
Keren Tazat, Susanne Schindler, Reinhard Deppeing, Nicola J Mabjeesh
We have shown previously that septin 9 isoform 1 (SEPT9_i1) protein associates with hypoxia-inducible factor (HIF)-1α to augment HIF-1 transcriptional activity by driving its importin-α-mediated nuclear translocation. Using in vitro and in vivo binding assays we identified that HIF-1α interacts with importin-α5 and importin-α7 in prostate cancer cells but only importin-α7 interacts with SEPT9_i1. The interaction with importin-α7 was dependent on the first 25 amino acids of SEPT9_i1 that are unique compared to other members of the mammalian septin family...
May 9, 2018: Cytoskeleton
Matt Greenlee, Annabel Alonso, Maliha Rahman, Nida Meednu, Kayla Davis, Victoria Tabb, River Cook, Rita K Miller
Stu2p is the yeast member of the XMAP215/Dis1/ch-TOG family of microtubule-associated proteins that promote microtubule polymerization. However, the factors that regulate its activity are not clearly understood. Here we report that Stu2p in the budding yeast Saccharomyces cerevisiae interacts with SUMO by covalent and non-covalent mechanisms. Stu2p interacted by two-hybrid analysis with the yeast SUMO Smt3p, its E2 Ubc9p, and the E3 Nfi1p. A region of Stu2p containing the dimerization domain was both necessary and sufficient for interaction with SUMO and Ubc9p...
May 5, 2018: Cytoskeleton
J Daniel Fenn, Paula C Monsma, Anthony Brown
Neurofilaments are flexible cytoskeletal polymers that are capable of folding and unfolding between their bouts of bidirectional movement along axons. Here we present a detailed characterization of this behavior in cultured neurons using kymograph analysis with 30 ms temporal resolution. We analyzed 781 filaments ranging from 0.6-42 µm in length. We observed complex behaviors including pinch folds, hairpin folds, orientation changes (flips), and occasional severing and annealing events. On average, the filaments spent approximately 40% of their time in some sort of folded configuration...
April 23, 2018: Cytoskeleton
Cynthia P Hsu, Behzad Moghadaszadeh, John H Hartwig, Alan H Beggs
The α-actinin proteins are a highly conserved family of actin crosslinkers that mediate interactions between several cytoskeletal and sarcomeric proteins. Nonsarcomeric α-actinin-1 and α-actinin-4 crosslink actin filaments in the cytoskeleton, while sarcomeric α-actinin-2 and α-actinin-3 serve a crucial role in anchoring actin filaments to the muscle Z-line. To assess the difference in turnover dynamics and structure/function properties between the α-actinin isoforms at the sarcomeric Z-line, we used Fluorescence Recovery After Photobleaching (FRAP) in primary myofiber cultures...
May 2018: Cytoskeleton
Sandeep M Nalluri, Joseph W O'Connor, Gage A Virgi, Samantha E Stewart, Dan Ye, Esther W Gomez
Epithelial-mesenchymal transition (EMT) is an important process that mediates organ development and wound healing, and in pathological contexts, it can contribute to the progression of fibrosis and cancer. During EMT, cells exhibit marked changes in cytoskeletal organization and increased expression of a variety of actin associated proteins. Here, we sought to determine the role of caldesmon in mediating EMT in response to transforming growth factor (TGF)-β1. We find that the expression level and phosphorylation state of caldesmon increase as a function of time following induction of EMT by TGFβ1 and these changes in caldesmon correlate with increased focal adhesion number and size and increased cell contractility...
May 2018: Cytoskeleton
Tianchen Hu, Philip V Bayly
It remains unclear how flagella generate propulsive, oscillatory waveforms. While it is well known that dynein motors, in combination with passive cytoskeletal elements, drive the bending of the axoneme by applying shearing forces and bending moments to microtubule doublets, the origin of rhythmicity is still mysterious. Most conceptual models of flagellar oscillation involve dynein regulation or switching, so that dynein activity first on one side of the axoneme, then the other, drives bending. In contrast, a "viscoelastic flutter" mechanism has recently been proposed, based on a dynamic structural instability...
May 2018: Cytoskeleton
Jiayan Guo, Hong Seok Kim, Reto Asmis, Richard F Ludueña
Microtubules are a major component of the neuronal cytoskeleton. Tubulin, the subunit protein of microtubules, is an α/β heterodimer. Both α and β exist as families of isotypes, whose members are encoded by different genes and have different amino acid sequences. The βII and βIII isotypes are very prominent in the nervous system. Our previous work has suggested that βII may play a role in neuronal differentiation, but the role of βIII in neurons is not well understood. In the work reported here, we examined the roles of the different β-tubulin isotypes in response to glutamate/glycine treatment, and found that both βII and βIII bind to glutathione in the presence of ROS, especially βIII...
April 16, 2018: Cytoskeleton
P W Gunning, E C Hardeman
No abstract text is available yet for this article.
April 2018: Cytoskeleton
Bipasha Barua, Maria Sckolnick, Howard D White, Kathleen M Trybus, Sarah E Hitchcock-DeGregori
Muscle contraction, cytokinesis, cellular movement, and intracellular transport depend on regulated actin-myosin interaction. Most actin filaments bind one or more isoform of tropomyosin, a coiled-coil protein that stabilizes the filaments and regulates interactions with other actin-binding proteins, including myosin. Isoform-specific allosteric regulation of muscle myosin II by actin-tropomyosin is well-established while that of processive myosins, such as myosin V, which transport organelles and macromolecules in the cell periphery, is less certain...
April 2018: Cytoskeleton
Syamalima Dube, Lynn Abbott, Samender Randhawa, Yingli Fan, Jushuo Wang, Jean M Sanger, Joseph W Sanger, Bernard J Poiesz, Dipak K Dube
Cloning and sequencing of various tropomyosin isoforms expressed in chickens have been described since the early 1980s. However, to the best of our knowledge, this is the first report on the molecular characterization and the expression of the sarcomeric isoform of the TPM3 gene in cardiac and skeletal muscles from developing as well as adult chickens. Expression of TPM3α was performed by conventional RT-PCR as well as qRT-PCR using relative expression (by ΔCT as well as ΔΔCT methods) and by determining absolute copy number...
April 2018: Cytoskeleton
Janice E Friend, Wasim A Sayyad, Rajesh Arasada, Chad D McCormick, John E Heuser, Thomas D Pollard
Myosin-II is required for the assembly and constriction of cytokinetic contractile rings in fungi and animals. We used electron microscopy, fluorescence recovery after photobleaching (FRAP), and fluorescence correlation spectroscopy (FCS) to characterize the physical properties of Myo2 from fission yeast Schizosaccharomyces pombe. By electron microscopy, Myo2 has two heads and a coiled-coiled tail like myosin-II from other species. The first 65 nm of the tail is a stiff rod, followed by a flexible, less-ordered region up to 30 nm long...
April 2018: Cytoskeleton
Harald Preisner, Jörn Habicht, Sriram G Garg, Sven B Gould
Metazoans evolved from a single protist lineage. While all eukaryotes share a conserved actin and tubulin-based cytoskeleton, it is commonly perceived that intermediate filaments (IFs), including lamin, vimentin or keratin among many others, are restricted to metazoans. Actin and tubulin proteins are conserved enough to be detectable across all eukaryotic genomes using standard phylogenetic methods, but IF proteins, in contrast, are notoriously difficult to identify by such means. Since the 1950s, dozens of cytoskeletal proteins in protists have been identified that seemingly do not belong to any of the IF families described for metazoans, yet, from a structural and functional perspective fit criteria that define metazoan IF proteins...
March 23, 2018: Cytoskeleton
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