Sliding between adjacent microtubules within the axonema gives rise to the motility of cilia and flagella. The driving force is produced by dynein complexes which are mainly composed of the axonemal dynein heavy chains. We used cells of human respiratory epithelium after in vitro ciliogenesis to clone cDNA fragments of nine dynein heavy chain genes, one of which had never been identified before. Dynein heavy chains are highly conserved from protozoa to human and the evolutionary ancestry of these dynein heavy chain cDNA fragments was deduced by phylogenetic analysis. These dynein heavy chain cDNAs are highly transcribed in human tissues containing axonema such as trachea, testis and brain, but not in adult heart or placenta. PAC clones containing dynein heavy chains were obtained and used to determine by FISH their chromosomal position in the human genome. They were mapped to 2p12-p11, 2q33, 3p21.2-p21.1, 13q14, 16p12 and 17p12. The chromosomal assignment of these dynein heavy chain genes which ...
During animal development cellular differentiation is often preceded by an asymmetric cell division whose polarity is determined by the orientation of the mitotic spindle. In the fruit fly, Drosophila melanogaster, the oocyte differentiates in a 16-cell syncytium that arises from a cystoblast which undergoes 4 synchronous divisions with incomplete cytokinesis. During these divisions, spindle orientation is highly ordered and is thought to impart a polarity to the cyst that is necessary for the subsequent differentiation of the oocyte. Using mutations in the Drosophila cytoplasmic dynein heavy chain gene, Dhc64C, we show that cytoplasmic dynein is required at two stages of oogenesis. Early in oogenesis, dynein mutations disrupt spindle orientation in dividing cysts and block oocyte determination. The localization of dynein in mitotic cysts suggests spindle orientation is mediated by the microtubule motor cytoplasmic dynein. Later in oogenesis, dynein function is necessary for proper ...
A novel Chlamydomonas flagellar mutant (oda-11) missing the alpha heavy chain of outer arm dynein but retaining the beta and gamma heavy chains was isolated. Restriction fragment length polymorphism analysis with an alpha heavy chain locus genomic probe indicated that the oda-11 mutation was genetically linked with the structural gene of the alpha heavy chain. In cross-section electron micrographs, the oda-11 axoneme lacked the outermost appendage of the outer arm, indicating that the alpha heavy chain should be located in this region in the wild-type outer arm. This mutant swam at 119 microns/s at 25 degrees C, i.e., at an intermediate speed between those of wild type (194 microns/s) and of oda-1 (62 microns/s), a mutant missing the entire outer dynein arm. The flagellar beat frequency (approximately 50 Hz) was also between those of wild type (approximately 60 Hz) and oda-1 (approximately 26 Hz). These results indicate that the outer dynein arm of Chlamydomonas can be assembled without the ...
The movement of cilia and flagella is powered by axonemal dyneins, a family of mechanoenzymes that convert the energy derived from ATP binding and hydrolysis into the sliding of adjacent outer doublet microtubules (Mitchell 1994; Witman et al. 1994; Porter 1996). Axonemal dyneins can be separated into two groups, the outer dynein arms and the inner dynein arms, which have different functions in generating and propagating the flagellar waveforms. The outer dynein arms provide power to the flagellar beat, as Chlamydomonas mutants lacking the outer arms generate normal waveforms, but swim with a reduced beat frequency (Mitchell and Rosenbaum 1985; Brokaw and Kamiya 1987). In contrast, the inner arms are essential for normal motility, as mutants with inner arm defects have near normal beat frequencies, but display aberrant waveforms (Brokaw and Kamiya 1987).. The Chlamydomonas outer arm is one of the most well characterized dynein complexes; it is composed of three dynein heavy chains (Dhc)1 (α, ...
We previously reported that the small nuclear RNA processing complex, Integrator, is required for dynein recruitment to the nuclear envelope at mitotic onset in cultured human cells. We now report an additional role for INT in ciliogenesis. Depletion of INT subunits from cultured human cells results in loss of primary cilia. We provide evidence that the requirements for INT in dynein localization and ciliogenesis are uncoupled: proteins essential for ciliogenesis are not essential for dynein recruitment to the nuclear envelope, while depletion of known regulators of perinuclear dynein has minimal effects on ciliogenesis. Taken together, our data support a model in which INT ensures proper processing of distinct pools of transcripts encoding components that independently promote perinuclear dynein enrichment and ciliogenesis.. ...
Outer-arm dynein purified from trout spermatozoa was disrupted by low-ionic-strength dialysis, and the resulting subunits were separated by sucrose density-gradient centrifugation. The intact 19 S dynein, containing the alpha- an beta-heavy chains, intermediate chains (ICs) 1-5 and light chains (LCs) 1-6, yielded several discrete particles: a 17.5 S adenosine triphosphatase (ATPase) composed of the alpha- and beta-chains ICs 3-5 and LC 1; a 9.5 S complex containing ICs 1 and 2 together with LCs 2, 3, 4, and 6; and a single light chain (LC 5), which sedimented at approximately 4 S. In some experiments, ICs 3-5 also separated from the heavy chain complex and were obtained as a distinct subunit. Further dissociation of the 17.5 S particle yielded a 13.1 S ATPase that contained the beta-heavy chain and ICs 3-5. The polypeptide compositions of the complexes provide new information on the intermolecular associations that occur within dynein. Substructural features of the trout dynein polypeptides also were
We have previously described the de novo evolution of a gene in the lineage of D. melanogaster (1). This gene, denoted Sdic, encodes a novel intermediate chain in a sperm-specific axonemal dynein. Changes that led to the creation of Sdic during the short evolutionary history of D. melanogaster [about 3 million years (2)] exhibit evidence for adaptive evolution. The gene was created from duplicated-and hence dispensable-copies of the genes for annexin X (AnnX) and the cytoplasmic dynein intermediate chain (Cdic). Three large deletions led to the fusion of the duplicated genes, whereupon a series of smaller deletions and nucleotide substitutions fashioned a new amino end of the Sdic polypeptide and created motifs characteristic of known axonemal dynein intermediate chains. The regulatory region of Sdic, including a spermatocyte-specific promoter element, also evolved fromAnnX and Cdic sequences (1).. In principle, the evolutionary changes in Sdic could have taken place relatively rapidly during ...
The cytoplasmic dynein complex is the major minus-end-directed microtubule motor. Although its directionality is evolutionary well conserved, differences exist among cytoplasmic dyneins from different species in their stepping behaviour, maximum velocity and force production. Recent experiments also suggest differences in processivity regulation. In the present article, we give an overview of dyneins motile properties, with a special emphasis on processivity and its regulation. Furthermore, we summarize recent findings of different pathways for microtubule plus-end loading of dynein. The present review highlights how distinct functions in different cell types or organisms appear to require different mechanochemical dynein properties and localization pathways. ...
The molecular mechanisms regulating cytoplasmic dynein‐mediated motility are not completely understood, but it is becoming increasingly clear that they involve multiple protein-protein interactions and post‐translational modifications. The dynactin complex, which can be linked to dynein through the interaction of its p150Glued subunit with DIC (Vaughan and Vallee, 1995), might play a role in dynein-cargo binding, e.g. by associating with spectrin (Muresan et al., 2001), and might regulate the processivity of the dynein motor (King and Schroer, 2000). However, dynein itself can also bind to (and transport) various cargoes through its light and light intermediate chains (Tai et al., 1999; Young et al., 2000). We envisage a function for mammalian BICD2 in dynein‐based transport that involves direct binding of BICD2 to the dynamitin subunit of dynactin and association with cytoplasmic dynein. These observations provide a molecular basis for the genetic evidence in D.melanogaster, which ...
We report here on the UV-induced vanadate-dependent cleavage of the alpha and beta heavy chains of the outer arm dynein from Chlamydomonas flagella. Both polypeptides are cleaved at a single site (termed the V1 site) by UV irradiation in the presence of Mg2+, ATP, and vanadate. The alpha chain yields fragments of Mr 290,000 and 190,000. Fragments of Mr 255,000 and 185,000 are obtained from the beta chain. Ultraviolet irradiation of the alpha and beta chains in the presence of vanadate and Mn2+ (but no nucleotide) induces cleavage of both molecules at sites (termed the V2 sites) distinct from the V1 sites. The single V2 site within the beta chain is located 75,000 daltons from the site of V1 cleavage within the Mr 255,000 V1 fragment. The alpha chain contains three distinct sites of V2 cleavage; all are located within the Mr 290,000 V1 fragment, 60,000, 90,000, and 100,000 daltons from the site of V1 cleavage. From these studies, we estimate the masses of the alpha and beta heavy chains to be 480,000 and
The highly motile, 9 + 0 sperm axoneme of Anguilla has inner dynein arms (IDAs) but not outer dynein arms. The in situ morphology of these IDAs is shown here to be essentially identical to the IDA morphology already seen in the axonemes of Chlamydomonas, Tetrahymena and Beroe, and in the sperm tails of echinoderms and several vertebrate species. In addition, this study demonstrates: (1) that the nexin (circumferential) links are present in Anguilla and are typical; (2) that IDA1 incorporates an archway, supported by a pillar-structure; (3) that images from thin sections and whole mounts are consistent with those from replicas of rapidly-frozen specimens; and (4) that the IDA and nexin link morphology is apparently unaffected by whether the axoneme is depleted of ATP, relaxed with ATP and vanadate, or inhibited by high ATP. An attempt has been made to reconcile the emergent morphology of the IDA complex with all earlier descriptions in the literature. From a detailed comparison of the results ...
Short Summary. Inside the cell, cargo-containing vesicles move on microtubules (MTs), powered by protein motors called kinesins and dyneins. Motor proteins work uni-directionally: dyneins transport vesicles inwards {into the cell (minus end of MTs)}, while kinesins move vesicles outwards, in the opposite direction.. This paper makes two points about inward vesicular trafficking: (1) that cholesterol-enriched domains (lipid rafts) help drive dynein motor clustering, a mechanism that helps dynein generate sufficient force for a one-way trip of a late phagasome to the lysosome and (2) that Leishmania donovani (causative agent of kala azhar), a successful intracellular pathogen, secretes lipids that disrupts lipid rafts, thus affecting dynein function and stonewalling the transport of the vesicle that contains it.. Phago-lysosomal fusion. Intracellular pathogens are ingested into vesicles called early endosomes that mature, by changing protein and lipid content, into late phagosomes. These finally ...
This work establishes Lis1 as a dynein regulatory protein and links its function to dynein enzymatic activity. The simplest interpretation of our data is that Lis1 acts specifically and directly on dynein. Although the increase in ATPase activity is modest at first glance, our determination that only one-third of the dynein molecules interacted with Lis1 suggests that there were two populations of motors present in the ATPase assay. The major population did not stably bind Lis1 and is not expected to have had any change in ATPase activity, whereas a smaller population binds Lis1, resulting in a boost in ATPase activity. In this scenario, the enzymatic activity of the dynein as a whole would have increased by only 40%, but the activity of Lis1-associated motors may have increased by ∼100%.. The finding that Lis1 can stimulate dynein in vitro supports our model that Lis1 has an activating influence on dynein in cells (Smith et al., 2000). In our previous work, we found that raising Lis1 ...
Mouse Monoclonal Anti-Dynein intermediate chain 2 Antibody (1C8) [DyLight 350]. Validated: WB, ELISA, ICC/IF. Tested Reactivity: Human, Canine. 100% Guaranteed.
Mouse Monoclonal Anti-Dynein intermediate chain 2 Antibody (1C8) [Alexa Fluor® 647]. Validated: WB, ELISA, ICC/IF. Tested Reactivity: Human, Canine. 100% Guaranteed.
The dynein intermediate chain (IC) is central to the structure of the dynein motor.2 It is composed of two domains. The extended N-terminal domain (N-IC), is indicated by grey solid and dotted lines. The C-terminal domain (C-IC), which interacts with the heavy chain, forms a relatively ordered and compact beta propeller structure indicated by the grey globular shapes in the figure.. Two copies of IC are present in every dynein motor, and the dimer is bridged by the three light chains LC8, LC7, and Tctex-1. In addition to the light chains, N-IC contains interaction motifs for several other proteins known to be integral to the function of dynein. These include p150Glued, the largest subunit of the dynein activator dynactin, and other proteins such as LIS1 and the ZW10 subunit of the Rod RZZ complex.. With its many interactions, N-IC appears to be the key modulator of dynein assembly and attachment to cargoes. With its extended structure, many interactions, and pivotal role in the function of a ...
TY - JOUR. T1 - The herpesvirus VP1/2 protein is an effector of dynein-mediated capsid transport and neuroinvasion. AU - Zaichick, Sofia V.. AU - Bohannon, Kevin P.. AU - Hughes, Ami. AU - Sollars, Patricia J.. AU - Pickard, Gary E.. AU - Smith, Gregory A.. PY - 2013/2/13. Y1 - 2013/2/13. N2 - Microtubule transport of herpesvirus capsids from the cell periphery to the nucleus is imperative for viral replication and, in the case of many alphaherpesviruses, transmission into the nervous system. Using the neuroinvasive herpesvirus, pseudorabies virus (PRV), we show that the viral protein 1/2 (VP1/2) tegument protein associates with the dynein/dynactin microtubule motor complex and promotes retrograde microtubule transport of PRV capsids. Functional activation of VP1/2 requires binding to the capsid protein pUL25 or removal of the capsid-binding domain. A proline-rich sequence within VP1/2 is required for the efficient interaction with the dynein/dynactin microtubule motor complex as well as for PRV ...
Positively regulates the activity of the minus-end directed microtubule motor protein dynein. Plays a central role in positioning the mitotic spindle at the bud neck during cell division. Targets cytoplasmic dynein to microtubule plus ends, thereby promoting dynein-mediated microtubule sliding along the bud cortex and consequently the movement of the mitotic spindle to the bud neck. Following plus end binding, dynein may be offloaded to the cortex by NUM1. Required for viability in the absence of the kinesin-related microtubule-dependent motor protein CIN8.
Nonpolarized cultured cells that adhere to the substrate on which they are growing orient their spindles parallel to the substratum, thereby allowing both daughter cells to maintain contact with the substrate. Interactions between the astral microtubules and various microtubule-organizing proteins, including the minus end-directed motor complex and the dynein-dynactin complex, are involved in connecting the spindle to the actin cytoskeleton and the cell cortex. Now Toyoshima et al. find that, in HeLa cells, integrin-mediated stimulation of phosphoinositide 3-kinase (PI3K) leading to the production of phosphatidylinositol 3,4,5-trisphosphate [PI(3,4,5)P3] at the midsection of the cell cortex in metaphase cells was required for proper spindle orientation. PI(3,4,5)P3 concentration was monitored with a green fluorescent protein fused to the pleckstrin homology domain of Akt (Akt-PH-GFP), and the midsection cortical localization, as well as proper spindle orientation, was lost if PI3K activity was ...
Abcam provides specific protocols for Anti-Dynein intermediate chain 1 antibody [74.1] (ab23905) : Flow cytometry protocols, Immunoprecipitation protocols…
Dyneins: Structure, Biology and Disease, Second Edition, offers a broad view of dyneins mechanics, dysfunction, and disease, providing an overview of dyn...
The EGFR ligand Spitz, which is crucial for several aspects of Drosophila development, is produced as an inactive membrane-bound precursor that is cleaved and activated in the Golgi or endosomal compartments. The essential transmembrane protein Star mediates the trafficking of the Spitz precursor, but what is the molecular basis of Stars activity? On page 2643, Thomas Hays and colleagues provide evidence that Star-directed transport of Spitz requires the activity of the microtubule-associated motor dynein and its activator dynactin. The authors show that Star disruption enhances the rough-eye phenotype in a fly strain that is mutant for Glued (a subunit of the dynactin complex), as well as in strains that have mutations in Dhc (which encodes the dynein heavy chain). Moreover, Star- and dynein-associated vesicles cofractionate in a partitioning assay. Importantly, overexpressing truncated Spitz (which mimics the activated protein) rescues the rough-eye phenotype of Glued-mutant flies. In S2 ...
Cytoplasmic dynein is the primary minus-end-directed microtubule (MT) motor. It is unclear how dynein coordinates ATP hydrolysis and MT attachment within and between its two motor domains, each containing four AAA+ ATPases (AAA: ATPase associated with various cellular activities), AAA1-4. We characterize how mechanical tension and nucleotide states of AAA1 and AAA3 regulate dynein-MT binding. Dynein binds MTs tighter when subjected to tension opposite its normal motility. ADP binding to AAA3 unexpectedly weakens MT-binding strength and reduces the bond strength anisotropy. Finally, AAA3 gates the activity of AAA1: ATP binding to AAA1 induces MT release only if AAA3 contains nucleotide. This work expands understanding of the role of force in dynein mechanochemistry and identifies regulatory functions of AAA3 ...
Summer Research Description: Dynein is an essential cytoskeletal motor protein, facilitating the transport of various materials within the cell by binding to and trafficking along microtubules. In non-dividing cells, dynein transports cargo from the cell periphery towards the nucleus and microtubule-organizing center, in a microtubule minus-end directed manner. Previous data indicates that dynein plays a role in HIV intracytoplasmic transport. In these studies, I used flow cytometry and X-gal analysis to assess the effects of Ciliobrevin, an inhibitor of dynein ATPase activity, on HIV infectivity. Using flow cytometry, I found that increasing the concentration of Ciliobrevin, gives an overall decrease in infectivity, however not to the extent shown by previous studies, likely due to differences in the approaches used to quantify the extent of infection. This increased inhibition of dynein leads to lowered infectivity because fewer HIV particles are being trafficked to the nucleus. I am also ...
DESCRIPTION (provided by applicant): Tumor cells that are resistant to the growth inhibitory effects of TGF? can still secrete TGF?, which enhances tumorigenesis via the paracrine effects of TGF? in the tumor microenvironment. It is advantageous to block this secreted TGF? in late-stage tumors that have lost the TGF? growth inhibitory signals. We have identified the signaling pathways mediating TGF?1 production in untransformed epithelial cells (UECs) and in human colon cancer cells (HCCCs). One of the differences involves a switching of the AP-1 transcription factors (TFs) bound to the relevant region of the TGF?1 promoter. Here we will explore the mechanisms underlying this TF switching, including the role played by altered compartmentalization of signaling complexes. In addition, we have identified the novel TGF? signaling intermediate km23, which is also a light chain of the motor protein dynein (DLC). The dynein motor complex can transport membrane vesicles (ie, endosomal compartments) ...
E3 ubiquitin ligase induced during late erythropoiesis. Directly binds and ubiquitinates the intermediate chain of the microtubule motor dynein (DYNC1LI1/DYNC1LI2), stimulating the degradation of the dynein holoprotein complex. May participate in the erythroblast enucleation process through regulation of nuclear polarization.
Short Summary. Inside the cell, cargo-containing vesicles move on microtubules (MTs), powered by protein motors called kinesins and dyneins. Motor proteins work uni-directionally: dyneins transport vesicles inwards {into the cell (minus end of MTs)}, while kinesins move vesicles outwards, in the opposite direction.. This paper makes two points about inward vesicular trafficking: (1) that cholesterol-enriched domains (lipid rafts) help drive dynein motor clustering, a mechanism that helps dynein generate sufficient force for a one-way trip of a late phagasome to the lysosome and (2) that Leishmania donovani (causative agent of kala azhar), a successful intracellular pathogen, secretes lipids that disrupts lipid rafts, thus affecting dynein function and stonewalling the transport of the vesicle that contains it.. Phago-lysosomal fusion. Intracellular pathogens are ingested into vesicles called early endosomes that mature, by changing protein and lipid content, into late phagosomes. These finally ...
PubMed comprises more than 30 million citations for biomedical literature from MEDLINE, life science journals, and online books. Citations may include links to full-text content from PubMed Central and publisher web sites.
PubMed comprises more than 30 million citations for biomedical literature from MEDLINE, life science journals, and online books. Citations may include links to full-text content from PubMed Central and publisher web sites.
Springer AL, Bruhn DF, Kinzel KW, Rosenthal NF, Zukas R, Klingbeil MM. 2011. Silencing of a putative inner arm dynein heavy chain results in flagellar immotility in Trypanosoma brucei.. Mol Biochem Parasitol. 175(1):68-75. ...
Springer AL, Bruhn DF, Kinzel KW, Rosenthal NF, Zukas R, Klingbeil MM. 2011. Silencing of a putative inner arm dynein heavy chain results in flagellar immotility in Trypanosoma brucei.. Mol Biochem Parasitol. 175(1):68-75. ...
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The blood sample should be taken 1.5 - 2 hours after a meal that includes protein. The foods chosen should reflect the usual main meal of the day and have regard for any dietary restrictions already in place. Failure to do this can lead to false negative findings. Please let me have the details of your GP and any diagnoses which you have been given so that I can write to him/her with the results of the test and my comments and suggestions for management. ...
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Note, the weight of an arm is substantial.. We therefore advise to use either arm rests to support the forearm or to put the arm on ...
It's been 24 years and I still miss my mom..I was 15 when she died in my arms on the way to the hospital..As suddenly and unexpectedly as an asthma attack and.....
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In this study, we describe the identification of a novel mutation in Dync1h1 in Swl/+ mice, which display an early-onset proprioceptive sensory neuropathy. Detailed comparison of Swl/+ mice with Loa/+ mice, another Dync1h1 mutant, demonstrate that both strains are characterized by a common proprioceptive sensory deficit. Thus, we provide in vivo evidence that dysfunction of cytoplasmic dynein can lead to an early-onset proprioceptive sensory neuropathy in mice.. Cytoplasmic dynein is the major microtubule minus end-directed motor protein, which is composed of two heavy chains (DYNC1H1), two intermediate chains, four light intermediate chains, and several light chains (Karki and Holzbaur, 1999; Hafezparast et al., 2003; Vallee et al., 2004). DYNC1H1 has a C-terminal motor domain head and an N-terminal cargo-binding domain stalk, and homodimerizes at the N-terminal. Most of the accessory subunits of cytoplasmic dynein associate with the N-terminal portion of DYNC1H1. Mediated by dynactin, a ...
Dynein intermediate chain 1, axonemal is a protein that in humans is encoded by the DNAI1 gene. The inner- and outer-arm dyneins, which bridge between the doublet microtubules in axonemes, are the force-generating proteins responsible for the sliding movement in axonemes. The intermediate and light chains, thought to form the base of the dynein arm, help mediate attachment and may also participate in regulating dynein activity. This gene encodes an intermediate chain dynein, belonging to the large family of motor proteins. Mutations in this gene result in abnormal ciliary ultrastructure and function associated with primary ciliary dyskinesia (PCD) and Kartagener syndrome. The DNAi1 gene (axonemal dynein intermediate chain 1 gene 1) is a gene involved in the development of proper respiratory function, motility of spermatozoa, and asymmetrical organization of the viscera during embryogenesis. This gene affects these three very different aspects of development because all three are dependent on ...
Human Usher syndrome (USH) is the most common form of combined deaf-blindness, characterized by profound congenital deafness, constant vestibular dysfunction and pre-pubertal onset of retinitis pigmentosa. The USH1G protein SANS (scaffold protein containing ankyrin repeats and SAM domain) is associated with microtubules and mediates a transport related periciliary protein network in photoreceptor cells. Here we aim to enlighten the involvement of SANS in ciliary transport of photoreceptor cells by identifying proteins associated with SANS in transport complexes. In Y2H screen of retinal cDNA library we identified the direct binding of SANS to dynactin-1 (p150Glued), a subunit of the dynactin complex and cargo linker to the cytoplasmic dynein motor. This interaction was validated in complementary interaction assays in vitro and in cell culture. In addition, we demonstrated the integration of SANS into the cytoplasmic dynein transport complex by GST-pull down of SANS with cytoplasmic dynein intermediate
Molecular analysis of LC7 from the Chlamydomonas outer dynein arm. (A) Two tryptic peptides from outer arm dynein LC7 were completely sequenced, yielding a tota
DYNC1LI1 antibody [2B6] (dynein, cytoplasmic 1, light intermediate chain 1) for FACS, ICC/IF, WB. Anti-DYNC1LI1 mAb (GTX84599) is tested in Human samples. 100% Ab-Assurance.
During mitosis, two arrays of microtubules form the bipolar mitotic spindle in order to effect partitioning of the duplicated chromosomes into the daughter cells. The fabrication of the spindle therefore is a key step in successful cell division, and a protein known as NuMA is needed to properly gather the ends of the microtubules at the poles.. Merdes et al. have found that, at the onset of mitosis, a complex of the microtubule motor protein dynein and dynactin powers NuMA transport along microtubules to the polar region. Transport and continued localization of NuMA at the pole is required to form and maintain an intact spindle, perhaps through binding of the individual microtubules to a NuMA multimer. Disruption of NuMA transport by addition of the dynactin inhibitor dynamitin, or by addition of anti-dynein antibodies, releases spindle microtubules from the tightly focused poles.-SMH. J. Cell Biol.149, 851 (2000).. ...
The gene mapt codes for the microtubule-associated protein Tau. The R406W amino acid substitution in Tau is associated with frontotemporal dementia with parkinsonism linked to chromosome 17 (FTDP-17) characterized by Tau-positive filamentous inclusions. These filamentous Tau inclusions are present i …
Supplementary Figure 1: The level of dynein light chain rp3 is unaffected by the overexpression of WT and mutant Tctex-1. Lysates of MDCK cells inducibly expressing Flag-rp3 and Tctex-1 (WT, S82A, S82E), either harvested from the uninduced (Dox+) or the induced (Dox-) condition, were separated by SDS-PAGE and immunoblotted with anti-rp3 antibody. rp3 was only detected in Flag-rp3-expressing lines cultured under the induced condition. Supplementary Figure 2: High-speed supernatants prepared from homogenates of induced MDCK cell lines were separated by velocity sedimentation on 5-20% sucrose gradients. Aliquots from all fractions were separated on SDS-PAGE and immunoblotted with the indicated Abs. For the endogenous Tctex-1 detection, protein blots were trimmed so that the regions containing Flag-Tctex-1 were removed to avoid antibody sequestration. Low levels of endogenous Tctex-1 were detected in the 19-20S dynein-containing fractions upon prolonged development. LC8 in MDCK cells was primarily ...
There are no specific protocols for Recombinant Human Dynein light chain protein (ab107140). Please download our general protocols booklet
Neurons are unique in that they are highly polarized cells with long projections. Motor neurons have axons that extend from the spinal cord out to the periphery to synapse with muscles; in the case of humans, these axons may extend for over a meter away from the cell body. Active transportation of proteins and organelles along the axon, in both directions between the cell body and the neuron synapse is essential for neuronal survival and communication. Anterograde axonal transport, from cell body to synapse, is undertaken by kinesins and other motor proteins. Retrograde axonal transport, from synapse to the cell body, is driven by the dynein motor within the dynein-dynactin complex. Defects in axonal transport have been shown to be present in mouse models of several neurodegenerative diseases, including Huntington disease, Alzheimer disease, and amyotrophic lateral sclerosis (ALS), and pathological findings such as axonal swellings that may be indicative of axonal transport defects have been ...
Indranil Banerjee and Yasuyuki Miyake were part of a research team of scientists from the ETH Zürich, the FMI and the Biological Research Center in Szeged (Hungary). They discovered a key aspect of influenza infection: the capsid of the influenza A virus imitates a bundle of protein waste. Individual protein wastes are trafficked to a larger aggregate called an aggresome. A cytoplasmic enzyme called histone deacetylase 6 (HDAC6) and cytoskeletal motor proteins dynein and myosin II are central to aggresome formation and its subsequent disassembly. By containing unanchored ubiquitin chains, the influenza virus loosely mimics protein waste, and takes advantage of aggresome-processing machinery to crack open its capsid and to release its RNA genome for infection. The scientists are now looking for compounds that prevent HDAC6 from binding to free ubiquitin. Such a compound could be the basis for novel influenza therapies ...