A novel microtubule-associated protein from mammalian nerve shows ATP-sensitive binding to microtubules.

Hollenbeck, Peter J.; Chapman, Kevin

doi:10.1083/jcb.103.4.1539

Cited by 38 publications

(14 citation statements)

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Section: Discussionmentioning

confidence: 96%

“…Cytoplasmic, dynein-like proteins unambiguously distinct from axonemal precursors have now been found in a variety of organisms [Hollenbeck and Chapman, 1986;Lye et al, 1987;Paschal et al, 1987;Euteneuer et al, 1988;Neeley and Boekelheide, 1988;Lye et al, 1989;Schnapp and Reese, 1989;Schroer et al, 19891. The broad phylogenetic distribution of this protein argues for a ubiquitous function, such as in organelle transport or mitosis. The immunofluorescence data reported here are consistent with cytoplasmic dynein's proposed function in organelle transport [Schroer et al, 1989;Schnapp and Reese, 1989;Vallee et al, 19891, in that the antibodies appear to label small cytoplasmic inclusions and the antigen is localized around the MTOC.…”

Section: Discussionmentioning

confidence: 99%

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Identification and immunolocalization of cytoplasmic dynein in dictyostelium

Koonce

McIntosh

1990

Cell Motil. Cytoskeleton

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A high molecular weight microtubule binding protein has been isolated from homogenates of Dictyostelium. Because of its sedimentation velocity (20s), ATP-sensitive binding to microtubules, UV-vanadate-ATP mediated fragmentation, prominent CTPase activity, and its ability to produce limited microtubule movement in vitro, we consider this protein to be a form of cytoplasmic dynein. A polyclonal antibody monospecific to this protein was produced, and dynein's intracellular distribution in ameboid cells was examined by immunofluorescence. The antibody labels a punctate cytoplasmic pattern, localizes to a spherical region adjacent to the nucleus, and also appears to label the nuclei. The punctate staining pattern is consistent with cytoplasmic dynein's proposed function in organelle transport. The spherical juxtanuclear object stained is coincident with this cell's microtubule organizing center, an obvious termination point for minus-end directed microtubule motors. By immunofluorescence, there does not appear to be a substantial amount of dynein in the intranuclear mitotic spindles of Dictyostelium. These data provide evidence for localization of cytoplasmic dynein in cells, and suggest that Dictyostelium will be a useful system in which to study the molecular biology of microtubule-associated motor enzymes.

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Section: Discussionmentioning

confidence: 96%

Section: Discussionmentioning

confidence: 99%

Identification and immunolocalization of cytoplasmic dynein in dictyostelium

Koonce

McIntosh

1990

Cell Motil. Cytoskeleton

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“…The fast axonal transport, by which various organelles are transported bidirectionally at their specific velocities, provides an ideal model system for studying this delivery system. Kinesin (4,49) and cytoplasmic dynein (21,32,42) were identified as candidates for motor proteins which transport membrane organelles along axonal microtubules anterogradely and retrogradely, respectively. Recently, several novel kinesin super family proteins (KIF proteins) were also proposed to account for the fast anterograde axo-# To whomcorrespondence should be addressed.…”

mentioning

confidence: 99%

Microtubule-associated Proteins Regulate Microtubule Function as the Track for Intracellular Membrane Organelle Transports.

Sato-Harada

Okabe

Umeyama

et al. 1996

Cell Struct. Funct.

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ABSTRACT. Axonal microtubules have two essential roles: providing the track for organelle transport and forming the cytoskeletal framework to maintain axonal morphology. Microtubule-associated proteins (MAPs) are essential for the formation of cytoskeletal architecture. However, they mayhave additional roles on the regulation of organelle transport by their interaction with motor proteins on the microtubules.Wefirst examined the effects of axonal MAPson the organelle movementalong microtubules in a heterologous system using COSfibroblasts, which express no axonal MAPs,such as tau or MAP2C. Transfection of tau or MAP2C gene suppressed organelle movement almost completely in this cell type, hence interaction of axonal MAPs with microtubules interferes with organelle transports. It is known that the phosphorylation of MAPsreduces their interaction with microtubules. In this sense, phosphorylation of MAPs can be a good candidate for the molecular switch to regulate the organelle transport. As a second set of experiments, we investigated the effects of modulating CAMP dependent protein kinase pathway on organelle transports in primary sensory neurons, where high-molecular-weight tau protein is the major MAP.Wefound that the application of dibutyryl CAMP enhanced transports of large organelles in the axon. Furthermore, this drug treatment phosphorylated endogenous tau protein and thus reduced the affinity of tau to microtubules.These results indicate that axonal MAPscan work as a phosphorylation-dependent regulator of organelle transport. Local activation of protein kinase pathways in the axon might play an important role on the segregation of microtubules serving for either organelle transport or cytoskeletal architecture.

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“…Sci. USA 85 (1988) for some other microtubule-associated proteins (28)(29)(30) was detected under these conditions. However, the structure presented in Fig.…”

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confidence: 86%

A 60-kDa cytoskeletal protein from Trypanosoma brucei brucei can interact with membranes and with microtubules.

Seebeck

Kung

Wyler

et al. 1988

Proc. Natl. Acad. Sci. U.S.A.

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The cytoskeleton of eukaryotic cells is a major determinant of cellular architecture and of many cellular functions. In addition to or in place of the transcellular cytoskeleton, many eukaryotic cells also contain membraneassociated cytoskeletal structures (membrane skeletons), which are important for cellular structure and function. The membrane skeleton of the parasitic hemoflagellate Trypanosoma brucei consists of a dense array of singlet microtubules (subpellicular microtubules), which are tightly associated to the overlying cell membrane. This study reports the identification of a microtubule-associated protein from Trypanosoma brucei that constitutes a component of the link between this microtubular array and the cell membrane. The protein can bind in vitro both to microtubules and to membrane vesicles or liposomes. Furthermore, it can crosslink microtubules and membrane vesicles, suggesting that it exerts a similar function in the membrane skeleton.Cytoskeletal structures that are intimately associated with the plasma membrane and that constitute essential functional components of the membrane have been identified in numerous eukaryotic cells. The membrane skeleton that has been studied in most detail is the spectrin network of the human erythrocyte (1-4). However, investigations of the membrane skeletons in many other cell types have revealed a wide variety in their composition and structure (5-9). In the parasitic hemoflagellate Trypanosoma brucei brucei, the entire plasma membrane is underpinned by a regular array of singlet microtubules (9)(10)(11)(12)(13)(14). This microtubular membrane skeleton forms the main structural component of the cell body. No transcellular cytoskeletal structures have yet been identified, suggesting that the microtubule-based membrane skeleton is the prime determinant of the cellular architecture. Very little is known of how these microtubules are connected to the overlying cell membrane. Recent studies have shown that the microtubules of the trypanosomal membrane skeleton are composed of similar tubulin isotypes as are, for example, those of the flagellar axoneme (9, 15). Analyses of the trypanosomal tubulin genes and their transcripts have also provided strong evidence that the multiple tubulin genes of T. brucei in fact give rise to only one isotype each of a-tubulin and of 8-tubulin (9,(16)(17)(18)(19). Thus, a direct interaction of the subpellicular microtubules with the overlying cell membrane via a particular membrane-specific tubulin isotype (20) or via a posttranslational modification of the tubulins (21) seems unlikely for the trypanosomal membrane skeleton.Consequently, microtubule-associated proteins may be required to mediate the contact between the microtubular array and the cell membrane. The contact between the microtubular array and the membrane can be disrupted in vivo by the action of chlorpromazine and related phenothiazines (22). A 60-kDa protein (p60) has been isolated from trypanosomes by chlorpromazine affinity chromatography, and monoclonal a...

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A novel microtubule-associated protein from mammalian nerve shows ATP-sensitive binding to microtubules.

Cited by 38 publications

References 38 publications

Identification and immunolocalization of cytoplasmic dynein in dictyostelium

Identification and immunolocalization of cytoplasmic dynein in dictyostelium

Microtubule-associated Proteins Regulate Microtubule Function as the Track for Intracellular Membrane Organelle Transports.

A 60-kDa cytoskeletal protein from Trypanosoma brucei brucei can interact with membranes and with microtubules.

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