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dynein light chain

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https://www.readbyqxmd.com/read/28214429/interplay-between-autophagy-and-apoptosis-in-selenium-deficient-cardiomyocytes-in-chicken
#1
Jie Yang, Yuan Zhang, Sattar Hamid, Jingzeng Cai, Qi Liu, Hao Li, Rihong Zhao, Hong Wang, Shiwen Xu, Ziwei Zhang
Dietary selenium (Se) deficiency can cause heart dysfunction, however the exact mechanism remains unclear. To understand this mechanism, 180day-old chicks, divided into two groups, C (control group) and L (low Se group), were fed with either a Se-sufficient (0.23mg/kg) or Se-deficient (0.033mg/kg) diets for 25days, respectively. Heart tissues and blood samples were collected. In L group, the activities of serum creatine kinase (CK) and creatine kinase-myoglobin (CK-MB) increased and typical ultrastructural apoptotic features were observed...
February 10, 2017: Journal of Inorganic Biochemistry
https://www.readbyqxmd.com/read/28003657/the-light-intermediate-chain-2-subpopulation-of-dynein-regulates-mitotic-spindle-orientation
#2
Sagar Mahale, Megha Kumar, Amit Sharma, Aswini Babu, Shashi Ranjan, Chetana Sachidanandan, Sivaram V S Mylavarapu
Cytoplasmic dynein 1 is a multi-protein intracellular motor essential for mediating several mitotic functions, including the establishment of proper spindle orientation. The functional relevance and mechanistic distinctions between two discrete dynein subpopulations distinguished only by Light Intermediate Chain (LIC) homologues, LIC1 and LIC2 is unknown during mitosis. Here, we identify LIC2-dynein as the major mediator of proper spindle orientation and uncover its underlying molecular mechanism. Cortically localized dynein, essential for maintaining correct spindle orientation, consists majorly of LIC2-dynein, which interacts with cortical 14-3-3 ε- ζ and Par3, conserved proteins required for orienting the spindle...
December 2016: Scientific Reports
https://www.readbyqxmd.com/read/27964786/dynein-light-chain-family-genes-in-15-plant-species-identification-evolution-and-expression-profiles
#3
Jun Cao, Xiangyang Li, Yueqing Lv
Dynein light chain (DLC) is one important component of the dynein complexes, which have been proved involving in a variety of cellular functions. However, higher plants lack all other components of the complexes except DLCs, suggesting that in plants, the DLC protein does not carry out the same function as it in animals. Therefore, the function of this family in plants is mysterious. In this study, we investigated the DLC gene family in 15 plant species and analyzed their expression profiles. In total, 128 DLC genes were identified from the 15 studied plant species and were divided into eight groups by their phylogenetic relation...
January 2017: Plant Science: An International Journal of Experimental Plant Biology
https://www.readbyqxmd.com/read/27864381/dynein-light-chain-dlc-1-promotes-localization-and-function-of-the-puf-protein-fbf-2-in-germline-progenitor-cells
#4
Xiaobo Wang, Jenessa R Olson, Dominique Rasoloson, Mary Ellenbecker, Jessica Bailey, Ekaterina Voronina
PUF family translational repressors are conserved developmental regulators, but the molecular function provided by the regions flanking the PUF RNA-binding domain is unknown. In C. elegans, the PUF proteins FBF-1 and FBF-2 support germline progenitor maintenance by repressing production of meiotic proteins and use distinct mechanisms to repress their target mRNAs. We identify dynein light chain DLC-1 as an important regulator of FBF-2 function. DLC-1 directly binds to FBF-2 outside of the RNA-binding domain and promotes FBF-2 localization and function...
December 15, 2016: Development
https://www.readbyqxmd.com/read/27861562/digitor-dasciz-has-multiple-roles-in-drosophila-development
#5
Saheli Sengupta, Uttama Rath, Changfu Yao, Michael Zavortink, Chao Wang, Jack Girton, Kristen M Johansen, Jørgen Johansen
In this study we provide evidence that the spindle matrix protein Skeletor in Drosophila interacts with the human ASCIZ (also known as ATMIN and ZNF822) ortholog, Digitor/dASCIZ. This interaction was first detected in a yeast two-hybrid screen and subsequently confirmed by pull-down assays. We also confirm a previously documented function of Digitor/dASCIZ as a regulator of Dynein light chain/Cut up expression. Using transgenic expression of a mCitrine-labeled Digitor construct, we show that Digitor/dASCIZ is a nuclear protein that is localized to interband and developmental puff chromosomal regions during interphase but redistributes to the spindle region during mitosis...
2016: PloS One
https://www.readbyqxmd.com/read/27858289/dynein-light-chain-dynll1-subunit-facilitates-porcine-circovirus-type-2-intracellular-transports-along-microtubules
#6
Sirin Theerawatanasirikul, Nantawan Phecharat, Chaiwat Prawettongsopon, Wanpen Chaicumpa, Porntippa Lekcharoensuk
Microtubule (MT) and dynein motor proteins facilitate intracytoplasmic transport of cellular proteins. Various viruses utilize microtubules and dynein for their movement from the cell periphery to the nucleus. The aim of this study was to investigate the intracellular transport of porcine circovirus type 2 (PCV2) via 8 kDa dynein light chain (DYNLL1, LC8) subunit along the MTs. At 20 μM, vinblastine sulfate inhibited tubulin polymerization resulting in disorganized morphology. In PCV2-infected PK-15 cells, double immunofluorescent labeling showed that the viral particles appeared at the cell periphery and gradually moved to the microtubule organization center (MTOC) at 0-12 hour post inoculation (hpi) while at 20-24 hpi they accumulated in the nucleus...
November 17, 2016: Archives of Virology
https://www.readbyqxmd.com/read/27823812/pex17p-dependent-assembly-of-pex14p-dyn2p-subcomplexes-of-the-peroxisomal-protein-import-machinery
#7
Anna Chan, Andreas Schummer, Sven Fischer, Thomas Schröter, Luis Daniel Cruz-Zaragoza, Julian Bender, Friedel Drepper, Silke Oeljeklaus, Wolf-H Kunau, Wolfgang Girzalsky, Bettina Warscheid, Ralf Erdmann
Peroxisomal matrix protein import is facilitated by cycling receptors that recognize their cargo proteins in the cytosol by peroxisomal targeting sequences (PTS). In the following, the assembled receptor-cargo complex is targeted to the peroxisomal membrane where it docks to the docking-complex as part of the peroxisomal translocation machinery. The docking-complex is composed of Pex13p, Pex14p and in yeast also Pex17p, whose function is still elusive. In order to characterize the function of Pex17p, we compared the composition and size of peroxisomal receptor-docking complexes from wild-type and pex17Δ cells...
December 2016: European Journal of Cell Biology
https://www.readbyqxmd.com/read/27776107/rasgrp1-deficiency-causes-immunodeficiency-with-impaired-cytoskeletal-dynamics
#8
Elisabeth Salzer, Deniz Cagdas, Miroslav Hons, Emily M Mace, Wojciech Garncarz, Özlem Yüce Petronczki, René Platzer, Laurène Pfajfer, Ivan Bilic, Sol A Ban, Katharina L Willmann, Malini Mukherjee, Verena Supper, Hsiang Ting Hsu, Pinaki P Banerjee, Papiya Sinha, Fabienne McClanahan, Gerhard J Zlabinger, Winfried F Pickl, John G Gribben, Hannes Stockinger, Keiryn L Bennett, Johannes B Huppa, Loïc Dupré, Özden Sanal, Ulrich Jäger, Michael Sixt, Ilhan Tezcan, Jordan S Orange, Kaan Boztug
RASGRP1 is an important guanine nucleotide exchange factor and activator of the RAS-MAPK pathway following T cell antigen receptor (TCR) signaling. The consequences of RASGRP1 mutations in humans are unknown. In a patient with recurrent bacterial and viral infections, born to healthy consanguineous parents, we used homozygosity mapping and exome sequencing to identify a biallelic stop-gain variant in RASGRP1. This variant segregated perfectly with the disease and has not been reported in genetic databases. RASGRP1 deficiency was associated in T cells and B cells with decreased phosphorylation of the extracellular-signal-regulated serine kinase ERK, which was restored following expression of wild-type RASGRP1...
December 2016: Nature Immunology
https://www.readbyqxmd.com/read/27744599/selenium-deficiency-induces-autophagy-in-immune-organs-of-chickens
#9
Pervez Ahmed Khoso, Tingru Pan, Na Wan, Zijiang Yang, Ci Liu, Shu Li
The aim of the present study was to investigate the effects of selenium (Se) deficiency on autophagy-related genes and on ultrastructural changes in the spleen, bursa of Fabricius, and thymus of chickens. The Se deficiency group was fed a basal diet containing Se at 0.033 mg/kg and the control group was fed the same basal diet containing Se at 0.15 mg/kg. The messenger RNA (mRNA) levels of the autophagy genes microtubule-associated protein 1 light chain 3 (LC3)-I, LC3-II, Beclin 1, dynein, autophagy associated gene 5 (ATG5), and target of rapamycin complex 1 (TORC1) were assessed using real-time qPCR...
October 15, 2016: Biological Trace Element Research
https://www.readbyqxmd.com/read/27693219/fhcabp1-fh22-a-fasciola-hepatica-calcium-binding-protein-with-ef-hand-and-dynein-light-chain-domains
#10
Sarah Cheung, Charlotte M Thomas, David J Timson
FH22 has been previously identified as a calcium-binding protein from the common liver fluke, Fasciola hepatica. It is part of a family of at least four proteins in this organism which combine an EF-hand containing N-terminal domain with a C-terminal dynein light chain-like domain. Here we report further biochemical properties of FH22, which we propose should be renamed FhCaBP1 for consistency with other family members. Molecular modelling predicted that the two domains are linked by a flexible region and that the second EF-hand in the N-terminal domain is most likely the calcium ion binding site...
November 2016: Experimental Parasitology
https://www.readbyqxmd.com/read/27646688/n-acetyl-d-glucosamine-kinase-interacts-with-dynein-lis1-nude1-complex-and-regulates-cell-division
#11
Syeda Ridita Sharif, Ariful Islam, Il Soo Moon
N-acetyl-D-glucosamine kinase (GlcNAc kinase or NAGK) primarily catalyzes phosphoryl transfer to GlcNAc during amino sugar metabolism. Recently, it was shown NAGK interacts with dynein light chain roadblock type 1 (DYNLRB1) and upregulates axo-dendritic growth, which is an enzyme activity-independent, non-canonical structural role. The authors examined the distributions of NAGK and NAGK-dynein complexes during the cell cycle in HEK293T cells. NAGK was expressed throughout different stages of cell division and immunocytochemistry (ICC) showed NAGK was localized at nuclear envelope, spindle microtubules (MTs), and kinetochores (KTs)...
September 2016: Molecules and Cells
https://www.readbyqxmd.com/read/27528745/a-mysterious-family-of-calcium-binding-proteins-from-parasitic-worms
#12
REVIEW
Charlotte M Thomas, David J Timson
There is a family of proteins from parasitic worms which combine N-terminal EF-hand domains with C-terminal dynein light chain-like domains. Data are accumulating on the biochemistry and cell biology of these proteins. However, little is known about their functions in vivo Schistosoma mansoni expresses 13 family members (SmTAL1-SmTAL13). Three of these (SmTAL1, SmTAL2 and SmTAL3) have been subjected to biochemical analysis which demonstrated that they have different molecular properties. Although their overall folds are predicted to be similar, small changes in the EF-hand domains result in differences in their ion binding properties...
August 15, 2016: Biochemical Society Transactions
https://www.readbyqxmd.com/read/27502274/molecular-basis-for-the-protein-recognition-specificity-of-the-dynein-light-chain-dynlt1-tctex1-characterization-of-the-interaction-with-activin-receptor-iib
#13
Javier Merino-Gracia, Héctor Zamora-Carreras, Marta Bruix, Ignacio Rodríguez-Crespo
It has been suggested that DYNLT1, a dynein light chain known to bind to various cellular and viral proteins, can function both as a molecular clamp and as a microtubule-cargo adapter. Recent data have shown that the DYNLT1 homodimer binds to two dynein intermediate chains to subsequently link cargo proteins such as the guanine nucleotide exchange factor Lfc or the small GTPases RagA and Rab3D. Although over 20 DYNLT1-interacting proteins have been reported, the exact sequence requirements that enable their association to the canonical binding groove or to the secondary site within the DYNLT1 surface are unknown...
September 30, 2016: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/27441562/dynein-light-intermediate-chain-2-facilitates-the-metaphase-to-anaphase-transition-by-inactivating-the-spindle-assembly-checkpoint
#14
Sagar P Mahale, Amit Sharma, Sivaram V S Mylavarapu
The multi-functional molecular motor cytoplasmic dynein performs diverse essential roles during mitosis. The mechanistic importance of the dynein Light Intermediate Chain homologs, LIC1 and LIC2 is unappreciated, especially in the context of mitosis. LIC1 and LIC2 are believed to exist in distinct cytoplasmic dynein complexes as obligate subunits. LIC1 had earlier been reported to be required for metaphase to anaphase progression by inactivating the kinetochore-microtubule attachment-sensing arm of the spindle assembly checkpoint (SAC)...
2016: PloS One
https://www.readbyqxmd.com/read/27433848/brca2-mediates-centrosome-cohesion-via-an-interaction-with-cytoplasmic-dynein
#15
Sadiya Malik, Hiroko Saito, Miho Takaoka, Yoshio Miki, Akira Nakanishi
BRCA2 is responsible for familial breast and ovarian cancer and has been linked to DNA repair and centrosome duplication. Here we analyzed the mechanism by which the centrosomal localization signal (CLS) of BRCA2 interacts with cytoplasmic dynein 1 to localize BRCA2 to the centrosome. In vitro pull-down assays demonstrated that BRCA2 directly binds to the cytoplasmic dynein 1 light intermediate chain 2. A dominant-negative HA-CLS-DsRed fusion protein, the depletion of dynein by siRNA, and the inactivation of dynein by EHNA, inhibited the localization of BRCA2 at centrosomes and caused the separation of centrosome pairs during the S-phase...
August 17, 2016: Cell Cycle
https://www.readbyqxmd.com/read/27251063/the-role-of-the-dynein-light-intermediate-chain-in-retrograde-ift-and-flagellar-function-in-chlamydomonas
#16
Jaimee Reck, Alexandria M Schauer, Kristyn VanderWaal Mills, Raqual Bower, Douglas Tritschler, Catherine A Perrone, Mary E Porter
The assembly of cilia and flagella depends on the activity of two microtubule motor complexes, kinesin-2 and dynein-2/1b, but the specific functions of the different subunits are poorly defined. Here we analyze Chlamydomonas strains expressing different amounts of the dynein 1b light intermediate chain (D1bLIC). Disruption of D1bLIC alters the stability of the dynein 1b complex and reduces both the frequency and velocity of retrograde intraflagellar transport (IFT), but it does not eliminate retrograde IFT...
August 1, 2016: Molecular Biology of the Cell
https://www.readbyqxmd.com/read/27170189/pdk1-akt-pathway-regulates-radial-neuronal-migration-and-microtubules-in-the-developing-mouse-neocortex
#17
Yasuhiro Itoh, Maiko Higuchi, Koji Oishi, Yusuke Kishi, Tomohiko Okazaki, Hiroshi Sakai, Takaki Miyata, Kazunori Nakajima, Yukiko Gotoh
Neurons migrate a long radial distance by a process known as locomotion in the developing mammalian neocortex. During locomotion, immature neurons undergo saltatory movement along radial glia fibers. The molecular mechanisms that regulate the speed of locomotion are largely unknown. We now show that the serine/threonine kinase Akt and its activator phosphoinositide-dependent protein kinase 1 (PDK1) regulate the speed of locomotion of mouse neocortical neurons through the cortical plate. Inactivation of the PDK1-Akt pathway impaired the coordinated movement of the nucleus and centrosome, a microtubule-dependent process, during neuronal migration...
May 24, 2016: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/27083189/fasciola-hepatica-calcium-binding-protein-fhcabp2-structure-of-the-dynein-light-chain-like-domain
#18
Thanh H Nguyen, Charlotte M Thomas, David J Timson, Mark J van Raaij
The common liver fluke Fasciola hepatica causes an increasing burden on human and animal health, partly because of the spread of drug-resistant isolates. As a consequence, there is considerable interest in developing new drugs to combat liver fluke infections. A group of potential targets is a family of calcium-binding proteins which combine an N-terminal domain with two EF-hand motifs and a C-terminal domain with predicted similarity to dynein light chains (DLC-like domain). The function of these proteins is unknown, although in several species, they have been localised to the tegument, an important structure at the host-parasite interface...
July 2016: Parasitology Research
https://www.readbyqxmd.com/read/26994403/p28-dynein-light-chains-and-ciliary-motility-in-tetrahymena-thermophila
#19
Aswati Subramanian, Amrita Kabi, Sean F Gray, David Pennock
Dynein light chains are required for the assembly of axonemal dyneins into cilia and flagella. Most organisms express a single p28 dynein light chain and four to nine one-headed inner arm dynein heavy chains. In contrast, Tetrahymena encodes three p28 dynein light chain genes (p28A, p28B, and p28C) and 18 one-headed inner arm dynein heavy chains. In this article it is shown that mutations in p28A and p28B affected both beat frequency and waveform of cilia, while mutations in p28C affected only ciliary beat frequency...
April 2016: Cytoskeleton
https://www.readbyqxmd.com/read/26923072/the-protein-inhibitor-of-nnos-pin-dlc1-lc8-binding-does-not-inhibit-the-nadph-dependent-heme-reduction-in-nnos-a-key-step-in-no-synthesis
#20
Swapnil S Parhad, Deepa Jaiswal, Krishanu Ray, Shyamalava Mazumdar
The neuronal nitric oxide synthase (nNOS) is an essential enzyme involved in the synthesis of nitric oxide (NO), a potent neurotransmitter. Although previous studies have indicated that the dynein light chain 1 (DLC1) binding to nNOS could inhibit the NO synthesis, the claim is challenged by contradicting reports. Thus, the mechanism of nNOS regulation remained unclear. nNOS has a heme-bearing, Cytochrome P450 core, and the functional enzyme is a dimer. The electron flow from NADPH to Flavin, and finally to the heme of the paired nNOS subunit within a dimer, is facilitated upon calmodulin (CaM) binding...
March 25, 2016: Biochemical and Biophysical Research Communications
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