Brain dynein (MAP1C) localizes on both anterogradely and retrogradely transported membranous organelles in vivo.

Hirokawa, Nobutaka; Sato-Yoshitake, Reiko; Yoshida, Toshimichi; Kawashima, Toshiyuki

doi:10.1083/jcb.111.3.1027

Cited by 249 publications

(175 citation statements)

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“…In fact, kinesin is primarily associated with anterogradely moving membranous organelles in the axon, strongly supporting the hypothesis that kinesin is really an anterograde motor in vivo (8). Brain dynein is associated with both anterogradely and retrogradely moving membranous organelles (9), consistent with the suggestion that brain dynein is transported to the nerve terminal by fast flow and subsequently functions as a retrograde transport motor in vivo. Molecular genetic and ultrastructural approaches have dissected the molecular structure and functional domains of kinesin motors (10)(11)(12).…”

supporting

confidence: 74%

The primary structure of rat brain (cytoplasmic) dynein heavy chain, a cytoplasmic motor enzyme.

Zhang

Tanaka

Nonaka

et al. 1993

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

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Overlapping cDNA clones encoding the heavy chain of rat brain cytoplasmic dynein have been isolated. The isolated cDNA clones contain an open reading frame of 13,932 bp encoding 4644 aa (Mr, 532,213). The deduced protein sequence of the heavy chain of rat brain dynein shows significant similarity to sea urchin flageilar -dynein (27.0% identical) and toDictyostelium cytoplasmic dynein (53.5% identical) throughout the entire sequence. The heavy chain of rat brain (cytoplasmic) dynein contains four putative nudeotide-binding consensus sequences [GX4GK(T/S)] in the central one-third region that are highly similar to those of sea urchin and Dictyostelium dyneins. The N-terminal one-third of the heavy chain of rat brain (cytoplasmic) dynein shows high similarity (43.8% identical) to that of Dictyostelium cytoplasmic dynein but poor similarity (19.4% identical) to that of sea urchin flageliar dynein. These results suggested that the C-terminal two-thirds of the dynein molecule is conserved and plays an essential role in microtubule-dependent motility activity, whereas the N-terminal regions are different between cytoplasmic and flageilar dyneins.The nerve cell develops a polarized morphology composed of highly branched dendrites, a long axon, and synapses. Because of the lack of protein synthesis machinery in the axon, proteins in the axon and synapses must be transported down the axon after being synthesized in the cell body. Many proteins are transported bidirectionally in membranous organelles of various kinds by fast axonal flow (200-400 mm/ day), whereas other proteins such as cytoskeletal components are conveyed by slow axonal flow (0.5-2 mm/day). Electron microscopic studies of the neuronal cytoskeleton in vivo have suggested that microtubules and crossbridges between microtubules and membranous organelles form the structural basis for fast flow (1-3). Recently, two microtubule-activated ATPases, kinesin and brain dynein [cytoplasmic dynein, microtubule-associated protein (MAP) 1C], were identified as candidates for anterograde and retrograde molecular motors, respectively (4-7). In fact, kinesin is primarily associated with anterogradely moving membranous organelles in the axon, strongly supporting the hypothesis that kinesin is really an anterograde motor in vivo (8). Brain dynein is associated with both anterogradely and retrogradely moving membranous organelles (9), consistent with the suggestion that brain dynein is transported to the nerve terminal by fast flow and subsequently functions as a retrograde transport motor in vivo. Molecular genetic and ultrastructural approaches have dissected the molecular structure and functional domains of kinesin motors (10-12). However, detailed analysis of the primary structure of brain dynein hasThe publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact. not yet been accomplished. To further elucidate the functi...

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supporting

confidence: 74%

The primary structure of rat brain (cytoplasmic) dynein heavy chain, a cytoplasmic motor enzyme.

Zhang

Tanaka

Nonaka

et al. 1993

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

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“…To elucidate KIF2's dynamics within axons, we observed its localization after ligating the peripheral (saphenous) nerves of adult mice. Our previous research has demonstrated that anterogradely and retrogradely transported membranous organelles, respectively, accumulate at the proximal and distal region of the ligated portion (Hirokawa et al, 1990. After 20 h of ligation, the KIF2 polyclonal antibody strongly stained the proximal region, though much less so the distal one (Fig.…”

Section: Localization Of Kif2 In Ligated Peripheral Nervesmentioning

confidence: 74%

KIF2 is a new microtubule-based anterograde motor that transports membranous organelles distinct from those carried by kinesin heavy chain or KIF3A/B.

Noda

Sato-Yoshitake

Kondo

et al. 1995

The Journal of Cell Biology

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Abstract. Kinesin is known as a representative cytoskeletal motor protein that is engaged in cell division and axonal transport. In addition to the mutant assay, recent advances using the PCR cloning technique have elucidated the existence of many kinds of kinesin-related proteins in yeast, Drosophila, and mice. We previously cloned five different members of kinesin superfamily proteins (KIFs) in mouse brain (Aizawa, H., Y. Sekine, R. Takemura, Z. Zhang, M. Nangaku, and N. . J. Cell Biol. 119:1287-1296 and demonstrated that one of them, KIF3A, is an anterograde motor (Kondo, S., R. SatoYashitake, Y. Noda, H. Aizawa, T. Nakata, Y. Matsuura, and N. Hirokawa. J. Cell Biol. 1994. 125:1095-1107. We have now characterized another axonal transport motor, KIF2. Different from other KIFs, KIF2 is a central type motor, since its motor domain is located in the center of the molecule.Recombinant KIF2 exists as a dimer with a bigger head and plus-end directionally moves microtubules at a velocity of 0.47 ± 0.11 /~m/s, which is two thirds that of kinesin's. Immunocytological examination showed that native KIF2 is abundant in developing axons and that it accumulates in the proximal region of the ligated nerves after a 20-h ligation. Soluble KIF2 exists without a light chain, and KIF2's associated-vesicles, immunoprecipitated by anti-KIF2 antibody, are different from those carried by existing motors such as kinesin and KIF3A. They are also distinct from synaptic vesicles, although KIF2 is accumulated in so-called synaptic vesicle fractions and embryonal growth cone particles. Our results strongly suggest that KIF2 functions as a new anterograde motor, being specialized for a particular group of membranous organelles involved in fast axonal transport. N'EURONS possess a highly polarized cytoarchitecture and transport system that enable them to perform their specialized functions. Especially within axons, each membrane or substrate is transported at the proper velocity and direction. Specialized markers have been used to identify many kinds of axonal transports, which can be roughly classified into several groups based on their velocities and directions (Grafstein and Forma, 1980;Dahlstrtm et al., 1992). The variety of cross-bridge structures connecting vesicles and microtubules also supports the existence of a plural mechanism for axonal transport (Hirokawa et al., 1982.Kinesin and cytoplasmic dynein are representative motors of anterograde and retrograde axonal transport, respectively (Vale et al., 1985;Brady et al., 1985;Paschal et al., 1987).Y. Noda and R. Sato-Yoshitake contributed equally to this study.Address all correspondence to Prof. N. Hirokawa, Department of Anatomy and Cell Biology, Faculty of Medicine, University of Tokyo, 7-3-1 Hongo, Tokyo 113, Japan. Ph.: (81)3-3812-2111 (ext. 3326), Fax: (81) 3-5689-4856.To better understand possible involvement of other motor molecules, we previously searched for new ones and ultimately applied the PCR method to clone five kinesin-like molecules (kinesin superfamily proteins ...

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“…These motors simultaneously bind to their cargo, which was shown in various cell systems, including fish and frog melanosomes (37), amoebas (38), lipid droplets in flies (14), intraflagellar transport in worms and algae (39,40), and vesicles in mammalian axons (41,42). The concurrent presence of kinesin and dynein is thought to be crucial for motor activity (3,13,43), but also recycles the motor back to MT plus ends (39,41). In fungi, kinesin-1 is thought to be involved in this process (26,30), making it likely that the observed anterograde motility of dynein is due to kinesin-1 activity.…”

Section: Discussionmentioning

confidence: 99%

“…In fungi, kinesin-1 is thought to be involved in this process (26,30), making it likely that the observed anterograde motility of dynein is due to kinesin-1 activity. It remains to be seen whether both motors directly interact (42) or attach to the same membranous cargo (41).…”

Section: Discussionmentioning

confidence: 99%

Transient binding of dynein controls bidirectional long-range motility of early endosomes

Schuster

Lipowsky

Assmann³

et al. 2011

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

141

258

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In many cell types, bidirectional long-range endosome transport is mediated by the opposing motor proteins dynein and kinesin-3. Here we use a fungal model system to investigate how both motors cooperate in early endosome (EE) motility. It was previously reported that Kin3, a member of the kinesin-3 family, and cytoplasmic dynein mediate bidirectional motility of EEs in the fungus Ustilago maydis. We fused the green fluorescent protein to the endogenous dynein heavy chain and the kin3 gene and visualized both motors and their cargo in the living cells. Whereas kinesin-3 was found on anterograde and retrograde EEs, dynein motors localize only to retrograde organelles. Live cell imaging shows that binding of retrograde moving dynein to anterograde moving endosomes changes the transport direction of the organelles. When dynein is leaving the EEs, the organelles switch back to anterograde kinesin-3-based motility. Quantitative photobleaching and comparison with nuclear pores as an internal calibration standard show that single dynein motors and four to five kinesin-3 motors bind to the organelles. These data suggest that dynein controls kinesin-3 activity on the EEs and thereby determines the longrange motility behavior of the organelles. membrane trafficking | modeling

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Brain dynein (MAP1C) localizes on both anterogradely and retrogradely transported membranous organelles in vivo.

Cited by 249 publications

References 54 publications

The primary structure of rat brain (cytoplasmic) dynein heavy chain, a cytoplasmic motor enzyme.

The primary structure of rat brain (cytoplasmic) dynein heavy chain, a cytoplasmic motor enzyme.

KIF2 is a new microtubule-based anterograde motor that transports membranous organelles distinct from those carried by kinesin heavy chain or KIF3A/B.

Transient binding of dynein controls bidirectional long-range motility of early endosomes

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