Mammalian cells express three distinct dynein heavy chains that are localized to different cytoplasmic organelles.

Vaisberg, Eugeni; Grissom, Paula M.; McIntosh, J. Richard

doi:10.1083/jcb.133.4.831

Cited by 195 publications

(229 citation statements)

References 46 publications

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“…The molecules that actually recruit and/or organize ␥-tubulin on Golgi membranes still remain to be identified. The assembly of ␥-tubulin onto centrosomes being mediated by cytoplasmic dynein in a MT-dependent manner (Young et al, 2000), one might even speculate that cytoplasmic dynein, which was also identified on Golgi membranes (Vaisberg et al, 1996;Roghi and Allan, 1999), might be needed to some extent for assembling and/or docking ␥-tubulin on the Golgi.…”

Section: Discussionmentioning

confidence: 99%

“…Dynamic and stable MTs are specialized in mediating specific transport steps (Mizuno and Singer, 1994;Poü s et al, 1998), which may involve various molecular motors, often localized on Golgi membranes (Vaisberg et al, 1996; for review see . The way such specialized motor proteins specifically interact with the appropriate target membranes is still an open question but may be related to the regulation of membrane traffic, as suggested by the example of rabkinesin-6, which binds the small GTPase Rab6 involved in Golgi-to-ER retrograde transport (Echard et al, 1998).…”

Section: Discussionmentioning

confidence: 99%

“…The binding of tubulin to Golgi membranes might also be due to an interaction with Golgi-resident proteins such as ␤-1,4-galactosyltransferase (Yamaguchi and Fukuda, 1995). Another possibility would be that very short tubulin polymers might interact with molecular motors constitutively bound to Golgi membranes (Vaisberg et al, 1996; for review, Hiro- Purified rat liver Golgi was washed as indicated with 2 M KCl and then rinsed three times in PEM buffer before being assayed for the presence of tubulins or to be used in the in vitro MT assembly assay. Samples were analyzed for the presence of tubulins by Western blotting, as described in Figure 7.…”

Section: Discussionmentioning

confidence: 99%

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The Golgi Complex Is a Microtubule-organizing Organelle

Chabin-Brion

Marceiller

Perez

et al. 2001

MBoC

277

245

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We show that the Golgi complex can directly stimulate microtubule nucleation in vivo and in vitro and thus behaves as a potent microtubule-organizing organelle in interphase cells. With the use of nocodazole wash-out experiments in hepatic cells, we found that the occurrence of noncentrosomal, early stabilized microtubules is highly correlated with the subcellular localization of Golgi membranes. With the use of in vitro reconstituted microtubule assembly systems with or without cytosol, we also found that, in contrast to centrosomally attached microtubules, the distal ends of Golgi-attached microtubules are remotely stabilized in a way that requires additional cytosolic component (s). Finally, we demonstrate that Golgi-based microtubule nucleation is direct and involves a subset of ␥-tubulin bound to the cytoplasmic face of the organelle. INTRODUCTIONIn interphase cells, the microtubule (MT) network plays a major role in membrane dynamics and organelle localization. In this context, the interaction between the Golgi complex and the MT network has been extensively studied. The Golgi apparatus colocalizes with the minus ends of MTs, which are usually associated with the centrosome (for review see Kreis et al., 1997;Thyberg and Moskalewski, 1999). This localization actually results from an equilibrium between two contradictory movements that have been unraveled with the use of MT-depolymerizing drugs and probably occur on MT subpopulations with different dynamics. The dispersal of Golgi elements occurs along stable MTs after depolymerization of the most labile MT population (Minin, 1997), whereas their reclustering involves newly assembled MTs (Ho et al., 1989). These contradictory movements of Golgi elements are mediated by distinct molecular motors. Consistent with earlier findings by Feiguin et al. (1994), who found that the expression of kinesin antisense oligonucleotide rendered the Golgi apparatus more compact, microinjection of antikinesin antibodies inhibited Golgi dispersion along stable, nocodazole-resistant MTs (Minin, 1997). Conversely, the central localization of the Golgi apparatus involves cytoplasmic dynein (Corthésy-Theulaz et al., 1992;Fath et al., 1994;Burkhardt et al., 1997;Harada et al., 1998). It is also worth noting that, in addition to the kinesin-mediated disruption of the central Golgi complex during MT depolymerization, the dispersion of Golgi elements also relies on the reconstitution of mini Golgi stacks at endoplasmic reticulum (ER) exit sites (Cole et al., 1996;Storrie et al., 1998). Such data on the scattering and the reclustering of the Golgi complex have led to the view that Golgi membranes undergo an intimate relationship with MTs and especially with a population of nocodazole-resistant, stable MTs. Stable MTs are characterized by the occurrence of posttranslationally modified tubulin-especially detyrosinated and acetylated tubulin (for review, see MacRae, 1997), which is thought to accumulate in stable MTs because of their longer half-lives, but does not influence MT stability i...

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

The Golgi Complex Is a Microtubule-organizing Organelle

Chabin-Brion

Marceiller

Perez

et al. 2001

MBoC

277

245

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“…6 Numerous distinct dynein heavy chain genes have been isolated from Paramecium, 7 Chlamydomonas, 8,9 sea urchin, 10 rat, 11,12 mouse, 13 and human. [13][14][15][16] However, comparing the dynein heavy chain gene family in well characterised species such as sea urchin suggests that either mammals have less axonemal dynein heavy genes or that some mammal genes are still to be discovered.…”

Section: Introductionmentioning

confidence: 99%

Identification, tissue specific expression, and chromosomal localisation of several human dynein heavy chain genes

Maiti

Matteï

Jorissen³

et al. 2000

Eur J Hum Genet

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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 was confirmed by GeneBridge 4 radiation hybrid screening, will be extremely useful for linkage analysis efforts in patients with primary ciliary dyskinesia (PCD). European Journal of Human Genetics (2000) 8, 923-932.

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“…The cytoplasmic dyneins are a multiprotein family of at least three members (Criswell et al, 1996;Vaisberg et al, 1996). The most abundant isoform, dynein 1, works in conjunction with a multisubunit activator protein, dynactin.…”

Section: Introductionmentioning

confidence: 99%

Role of Dynactin in Endocytic Traffic: Effects of Dynamitin Overexpression and Colocalization with CLIP-170

Valetti

Wetzel

Schrader

et al. 1999

MBoC

257

252

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The flow of material from peripheral, early endosomes to late endosomes requires microtubules and is thought to be facilitated by the minus end-directed motor cytoplasmic dynein and its activator dynactin. The microtubule-binding protein CLIP-170 may also play a role by providing an early link to endosomes. Here, we show that perturbation of dynactin function in vivo affects endosome dynamics and trafficking. Endosome movement, which is normally bidirectional, is completely inhibited. Receptor-mediated uptake and recycling occur normally, but cells are less susceptible to infection by enveloped viruses that require delivery to late endosomes, and they show reduced accumulation of lysosomally targeted probes. Dynactin colocalizes at microtubule plus ends with CLIP-170 in a way that depends on CLIP-170’s putative cargo-binding domain. Overexpression studies using p150Glued, the microtubule-binding subunit of dynactin, and mutant and wild-type forms of CLIP-170 indicate that CLIP-170 recruits dynactin to microtubule ends. These data suggest a new model for the formation of motile complexes of endosomes and microtubules early in the endocytic pathway.

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Mammalian cells express three distinct dynein heavy chains that are localized to different cytoplasmic organelles.

Cited by 195 publications

References 46 publications

The Golgi Complex Is a Microtubule-organizing Organelle

The Golgi Complex Is a Microtubule-organizing Organelle

Identification, tissue specific expression, and chromosomal localisation of several human dynein heavy chain genes

Role of Dynactin in Endocytic Traffic: Effects of Dynamitin Overexpression and Colocalization with CLIP-170

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