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Dynactin

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https://www.readbyqxmd.com/read/29913154/interactions-between-monomeric-cct%C3%AE-and-p150-glued-a-novel-function-for-cct%C3%AE-at-the-cell-periphery-distinct-from-the-protein-folding-activity-of-the-molecular-chaperone-cct
#1
Meriem Echbarthi, Josefine Vallin, Julie Grantham
Chaperonin containing tailless complex polypeptide 1 (CCT) is a molecular chaperone consisting of eight distinct protein subunits, that when oligomeric is essential for the folding of newly synthesized tubulin and actin. In addition to folding, CCT activity includes functions of individual subunits in their monomeric form. For example, when CCTδ monomer levels are increased in cultured mammalian cells, numerous cell surface protrusions are formed from retraction fibres, indicating that an underlying function for the CCTδ monomer exists...
June 15, 2018: Experimental Cell Research
https://www.readbyqxmd.com/read/29910809/sailing-to-and-docking-at-the-immune-synapse-role-of-tubulin-dynamics-and-molecular-motors
#2
REVIEW
Noa Beatriz Martín-Cófreces, Francisco Sánchez-Madrid
The different cytoskeleton systems and their connecting molecular motors move vesicles and intracellular organelles to shape cells. Polarized cells with specialized functions display an exquisite spatio-temporal regulation of both cytoskeletal and organelle arrangements that support their specific tasks. In particular, T cells rapidly change their shape and cellular function through the establishment of cell surface and intracellular polarity in response to a variety of cues. This review focuses on the contribution of the microtubule-based dynein/dynactin motor complex, the tubulin and actin cytoskeletons, and different organelles to the formation of the antigen-driven immune synapse...
2018: Frontiers in Immunology
https://www.readbyqxmd.com/read/29895958/unc-16-jip3-and-unc-76-fez1-limit-the-density-of-mitochondria-in-c-elegans-neurons-by-maintaining-the-balance-of-anterograde-and-retrograde-mitochondrial-transport
#3
Guruprasada Reddy Sure, Anusheela Chatterjee, Nikhil Mishra, Vidur Sabharwal, Swathi Devireddy, Anjali Awasthi, Swetha Mohan, Sandhya P Koushika
We investigate the role of axonal transport in regulating neuronal mitochondrial density. We show that the density of mitochondria in the touch receptor neuron (TRN) of adult Caenorhabditis elegans is constant. Mitochondrial density and transport are controlled both by the Kinesin heavy chain and the Dynein-Dynactin complex. However, unlike in other models, the presence of mitochondria in C. elegans TRNs depends on a Kinesin light chain as well. Mutants in the three C. elegans miro genes do not alter mitochondrial density in the TRNs...
June 12, 2018: Scientific Reports
https://www.readbyqxmd.com/read/29869045/assessing-the-impact-of-electrostatic-drag-on-processive-molecular-motor-transport
#4
J Darby Smith, Scott A McKinley
The bidirectional movement of intracellular cargo is usually described as a tug-of-war among opposite-directed families of molecular motors. While tug-of-war models have enjoyed some success, recent evidence suggests underlying motor interactions are more complex than previously understood. For example, these tug-of-war models fail to predict the counterintuitive phenomenon that inhibiting one family of motors can decrease the functionality of opposite-directed transport. In this paper, we use a stochastic differential equations modeling framework to explore one proposed physical mechanism, called microtubule tethering, that could play a role in this "co-dependence" among antagonistic motors...
June 4, 2018: Bulletin of Mathematical Biology
https://www.readbyqxmd.com/read/29864111/prognostic-value-of-dynactin-mrna-expression-in-cutaneous-melanoma
#5
Qiaoqi Wang, Xiangkun Wang, Qian Liang, Shijun Wang, Xiwen Liao, Dong Li, Fuqiang Pan
BACKGROUND Dynactin (DCTN) is a multi-subunit protein encoded by DCTN genes for 6 subunits. In different diseases the DCTN genes may have different roles; therefore, we investigated the prognostic potential of DCTN mRNA expression in cutaneous melanoma (CM). MATERIAL AND METHODS Data for DCTN mRNA expression in CM patients were obtained from the OncoLnc database, which contains updated gene expression data for 459 CM patients based on the Cancer Genome Atlas. Kaplan-Meier analysis and a Cox regression model were used to determine overall survival (OS) with calculation of hazard ratios (HRs) and 95% confidence intervals (CIs)...
June 4, 2018: Medical Science Monitor: International Medical Journal of Experimental and Clinical Research
https://www.readbyqxmd.com/read/29848445/dynein-dynactin-numa-clusters-generate-cortical-spindle-pulling-forces-as-a-multi-arm-ensemble
#6
Masako Okumura, Toyoaki Natsume, Masato T Kanemaki, Tomomi Kiyomitsu
To position the mitotic spindle within the cell, dynamic plus ends of astral microtubules are pulled by membrane-associated cortical force-generating machinery. However, in contrast to the chromosome-bound kinetochore structure, how the diffusion-prone cortical machinery is organized to generate large spindle-pulling forces remains poorly understood. Here, we develop a light-induced reconstitution system in human cells. We find that induced cortical targeting of NuMA, but not dynein, is sufficient for spindle pulling...
May 31, 2018: ELife
https://www.readbyqxmd.com/read/29685992/spindly-is-required-for-rapid-migration-of-human-cells
#7
Claudia Conte, Michelle A Baird, Michael W Davidson, Eric R Griffis
Dynein is the sole processive minus-end-directed microtubule motor found in animals. It has roles in cell division, membrane trafficking, and cell migration. Together with dynactin, dynein regulates centrosomal orientation to establish and maintain cell polarity, controls focal adhesion turnover and anchors microtubules at the leading edge. In higher eukaryotes, dynein/dynactin requires additional components such as Bicaudal D to form an active motor complex and for regulating its cellular localization. Spindly is a protein that targets dynein/dynactin to kinetochores in mitosis and can activate its motility in vitro However, no role for Spindly in interphase dynein/dynactin function has been found...
May 29, 2018: Biology Open
https://www.readbyqxmd.com/read/29679050/misp-regulates-the-iqgap1-cdc42-complex-to-collectively-orchestrate-spindle-orientation-and-mitotic-progression
#8
Barbara Vodicska, Berati Cerikan, Elmar Schiebel, Ingrid Hoffmann
Precise mitotic spindle orientation is essential for both cell fate and tissue organization while defects in this process are associated with tumorigenesis and other diseases. In most animal cell types, the dynein motor complex is anchored at the cell cortex and exerts pulling forces on astral microtubules to position the spindle. The actin-binding protein MISP controls spindle orientation and mitotic progression in human cells. However, the exact underlying mechanism remains to be elucidated. Here we report that MISP interacts with the multidomain scaffolding protein IQGAP1...
April 20, 2018: Scientific Reports
https://www.readbyqxmd.com/read/29669740/activated-ezrin-controls-misp-levels-to-ensure-correct-numa-polarization-and-spindle-orientation
#9
Yvonne T Kschonsak, Ingrid Hoffmann
Correct spindle orientation is achieved through signaling pathways that provide a molecular link between the cell cortex and spindle microtubules in an F-actin-dependent manner. A conserved cortical protein complex, composed of LGN (also known as GPSM2), NuMA (also known as NUMA1) and dynein-dynactin, plays a key role in establishing proper spindle orientation. It has also been shown that the actin-binding protein MISP and the ERM family, which are activated by lymphocyte-oriented kinase (LOK, also known as STK10) and Ste20-like kinase (SLK) (hereafter, SLK/LOK) in mitosis, regulate spindle orientation...
May 21, 2018: Journal of Cell Science
https://www.readbyqxmd.com/read/29662141/the-cytoplasmic-dynein-transport-machinery-and-its-many-cargoes
#10
REVIEW
Samara L Reck-Peterson, William B Redwine, Ronald D Vale, Andrew P Carter
Cytoplasmic dynein 1 is an important microtubule-based motor in many eukaryotic cells. Dynein has critical roles both in interphase and during cell division. Here, we focus on interphase cargoes of dynein, which include membrane-bound organelles, RNAs, protein complexes and viruses. A central challenge in the field is to understand how a single motor can transport such a diverse array of cargoes and how this process is regulated. The molecular basis by which each cargo is linked to dynein and its cofactor dynactin has started to emerge...
June 2018: Nature Reviews. Molecular Cell Biology
https://www.readbyqxmd.com/read/29615558/requirement-of-the-dynein-adaptor-spindly-for-mitotic-and-post-mitotic-functions-in-drosophila
#11
Giuliana D Clemente, Matthew R Hannaford, Hamze Beati, Katja Kapp, Jens Januschke, Eric R Griffis, Hans-Arno J Müller
Spindly was originally identified as a specific regulator of Dynein activity at the kinetochore. In early prometaphase, Spindly recruits the Dynein/Dynactin complex, promoting the establishment of stable kinetochore-microtubule interactions and progression into anaphase. While details of Spindly function in mitosis have been worked out in cultured human cells and in the C. elegans zygote, the function of Spindly within the context of an organism has not yet been addressed. Here, we present loss- and gain-of-function studies of Spindly using transgenic RNAi in Drosophila ...
March 30, 2018: Journal of Developmental Biology
https://www.readbyqxmd.com/read/29579703/backbone-amide-15-n-chemical-shift-tensors-report-on-hydrogen-bonding-interactions-in-proteins-a-magic-angle-spinning-nmr-study
#12
Sivakumar Paramasivam, Angela M Gronenborn, Tatyana Polenova
Chemical shift tensors (CSTs) are an exquisite probe of local geometric and electronic structure. 15 N CST are very sensitive to hydrogen bonding, yet they have been reported for very few proteins to date. Here we present experimental results and statistical analysis of backbone amide 15 N CSTs for 100 residues of four proteins, two E. coli thioredoxin reassemblies (1-73-(U-13 C,15 N)/74-108-(U-15 N) and 1-73-(U-15 N)/74-108-(U-13 C,15 N)), dynein light chain 8 LC8, and CAP-Gly domain of the mammalian dynactin...
August 2018: Solid State Nuclear Magnetic Resonance
https://www.readbyqxmd.com/read/29528393/novel-insights-into-smaled2-bicd2-mutations-increase-microtubule-stability-and-cause-defects-in-axonal-and-nmj-development
#13
Lilian A Martinez Carrera, Elke Gabriel, Colin D Donohoe, Irmgard Hölker, Aruljothi Mariappan, Markus Storbeck, Mirka Uhlirova, Jay Gopalakrishnan, Brunhilde Wirth
Bicaudal D2 (BICD2) encodes a highly conserved motor adaptor protein that regulates the dynein-dynactin complex in different cellular processes. Heterozygous mutations in BICD2 cause autosomal dominant lower extremity-predominant spinal muscular atrophy-2 (SMALED2). Although, various BICD2 mutations have been shown to alter interactions with different binding partners or the integrity of the Golgi apparatus, the specific pathological effects of BICD2 mutations underlying SMALED2 remain elusive. Here, we show that the fibroblasts derived from individuals with SMALED2 exhibit stable microtubules...
May 15, 2018: Human Molecular Genetics
https://www.readbyqxmd.com/read/29515126/a-conserved-interaction-of-the-dynein-light-intermediate-chain-with-dynein-dynactin-effectors-necessary-for-processivity
#14
In-Gyun Lee, Mara A Olenick, Malgorzata Boczkowska, Clara Franzini-Armstrong, Erika L F Holzbaur, Roberto Dominguez
Cytoplasmic dynein is the major minus-end-directed microtubule-based motor in cells. Dynein processivity and cargo selectivity depend on cargo-specific effectors that, while generally unrelated, share the ability to interact with dynein and dynactin to form processive dynein-dynactin-effector complexes. How this is achieved is poorly understood. Here, we identify a conserved region of the dynein Light Intermediate Chain 1 (LIC1) that mediates interactions with unrelated dynein-dynactin effectors. Quantitative binding studies map these interactions to a conserved helix within LIC1 and to N-terminal fragments of Hook1, Hook3, BICD2, and Spindly...
March 7, 2018: Nature Communications
https://www.readbyqxmd.com/read/29490687/genetic-ablation-of-dynactin-p150-glued-in-postnatal-neurons-causes-preferential-degeneration-of-spinal-motor-neurons-in-aged-mice
#15
Jia Yu, Chen Lai, Hoon Shim, Chengsong Xie, Lixin Sun, Cai-Xia Long, Jinhui Ding, Yan Li, Huaibin Cai
BACKGROUND: Dynactin p150Glued , the largest subunit of the dynactin macromolecular complex, binds to both microtubules and tubulin dimers through the N-terminal cytoskeleton-associated protein and glycine-rich (CAP-Gly) and basic domains, and serves as an anti-catastrophe factor in stabilizing microtubules in neurons. P150Glued also initiates dynein-mediated axonal retrograde transport. Multiple missense mutations at the CAP-Gly domain of p150Glued are associated with motor neuron diseases and other neurodegenerative disorders, further supporting the importance of microtubule domains (MTBDs) in p150Glued functions...
March 1, 2018: Molecular Neurodegeneration
https://www.readbyqxmd.com/read/29476122/author-correction-cryo-electron-tomography-reveals-that-dynactin-recruits-a-team-of-dyneins-for-processive-motility
#16
Danielle A Grotjahn, Saikat Chowdhury, Yiru Xu, Richard J McKenney, Trina A Schroer, Gabriel C Lander
In the version of this article initially published online, an incorrect accession code, EMD-5NW4, was introduced on page 1 of the article PDF, in section 'BICD2N mediates the association of two dynein dimers with a single dynactin'. This has been corrected to PDB 5NW4. The error has been corrected in the PDF and HTML versions of this article.
April 2018: Nature Structural & Molecular Biology
https://www.readbyqxmd.com/read/29420470/cryo-em-shows-how-dynactin-recruits-two-dyneins-for-faster-movement
#17
Linas Urnavicius, Clinton K Lau, Mohamed M Elshenawy, Edgar Morales-Rios, Carina Motz, Ahmet Yildiz, Andrew P Carter
Dynein and its cofactor dynactin form a highly processive microtubule motor in the presence of an activating adaptor, such as BICD2. Different adaptors link dynein and dynactin to distinct cargoes. Here we use electron microscopy and single-molecule studies to show that adaptors can recruit a second dynein to dynactin. Whereas BICD2 is biased towards recruiting a single dynein, the adaptors BICDR1 and HOOK3 predominantly recruit two dyneins. We find that the shift towards a double dynein complex increases both the force and speed of the microtubule motor...
February 7, 2018: Nature
https://www.readbyqxmd.com/read/29416113/cryo-electron-tomography-reveals-that-dynactin-recruits-a-team-of-dyneins-for-processive-motility
#18
Danielle A Grotjahn, Saikat Chowdhury, Yiru Xu, Richard J McKenney, Trina A Schroer, Gabriel C Lander
Cytoplasmic dynein is a protein complex that transports molecular cargo along microtubules (MTs), playing a key role in the intracellular trafficking network. Vertebrate dynein's movement becomes strikingly enhanced upon interacting with dynactin and a cargo adaptor such as BicaudalD2. However, the mechanisms responsible for increased transport activity are not well understood, largely owing to limited structural information. We used cryo-electron tomography (cryo-ET) to visualize the 3D structure of the MT-bound dynein-dynactin complex from Mus musculus and show that the dynactin-cargo adaptor complex binds two dimeric dyneins...
March 2018: Nature Structural & Molecular Biology
https://www.readbyqxmd.com/read/29401420/cooperative-accumulation-of-dynein-dynactin-at-microtubule-minus-ends-drives-microtubule-network-reorganization
#19
Ruensern Tan, Peter J Foster, Daniel J Needleman, Richard J McKenney
Cytoplasmic dynein-1 is a minus-end-directed motor protein that transports cargo over long distances and organizes the intracellular microtubule (MT) network. How dynein motor activity is harnessed for these diverse functions remains unknown. Here, we have uncovered a mechanism for how processive dynein-dynactin complexes drive MT-MT sliding, reorganization, and focusing, activities required for mitotic spindle assembly. We find that motors cooperatively accumulate, in limited numbers, at MT minus-ends. Minus-end accumulations drive MT-MT sliding, independent of MT orientation, resulting in the clustering of MT minus-ends...
January 22, 2018: Developmental Cell
https://www.readbyqxmd.com/read/29273399/behavioral-defects-in-a-dctn1-g71a-transgenic-mouse-model-of-perry-syndrome
#20
Takayasu Mishima, Manami Deshimaru, Takuya Watanabe, Kaori Kubota, Mariko Kinoshita-Kawada, Junichi Yuasa-Kawada, Kotaro Takasaki, Yoshinari Uehara, Shozo Jinno, Katsunori Iwasaki, Yoshio Tsuboi
Perry syndrome is a rare neurodegenerative disease characterized by parkinsonism, depression/apathy, weight loss, and central hypoventilation. Our previously-conducted genome-wide association scan and subsequent studies identified nine mutations in DCTN1, the largest protein subunit of the dynactin complex, in patients with Perry syndrome. These included G71A in the microtubule-binding cytoskeleton-associated protein Gly-rich domain of p150Glued . The dynactin complex is essential for function of the microtubule-based cytoplasmic retrograde motor dynein...
February 14, 2018: Neuroscience Letters
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