GMAP-210, A Cis-Golgi Network-associated Protein, Is a Minus End Microtubule-binding Protein

Infante, Carlos; Ramos‐Morales, Francisco; Fedriani, Concepción; Bornens, Michel; Rı́os, Rosa M.

doi:10.1083/jcb.145.1.83

Cited by 155 publications

(149 citation statements)

References 60 publications

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Section: Discussionmentioning

confidence: 99%

“…A similar model might also apply for the Golgi complex in which the Golgi-associated MAP GMAP-210 that was shown to bind both the minus end of MTs and CGN membranes (Infante et al, 1999) would be a good docking candidate. Additionally, the MT-stabilizing effect of Golgi membranes and the fact that GMAP associates with a subset of stable MTs in vivo (Infante et al, 1999) might also fit well with this hypothesis. In this respect, the in vitro system we used to reconstitute the MTstabilizing effect only reproduced plus-end dynamics, which is necessary and sufficient to restore the sensitivity of MTs to nocodazole (Saoudi et al, 1998).…”

Section: Discussionmentioning

confidence: 99%

“…Consistently, it has been shown that other biological membranes such as fish melanophore pigment granules and fish fibroblast membranes can readily nucleate MTs in vivo Kaverina et al, 1998) or that the apical membrane of polarized epithelial cells participate in the organization of the interphase MT network (Meads and Schroer, 1995). Regarding MT stabilization, the recent identification of the cis-Golgi network (CGN)-associated MT-associated protein GMAP-210, and its association with a hyperstable population of detyrosinated MTs are also in favor of Golgi-mediated MT stabilization (Infante et al, 1999).In this study, we show that in addition to the centrosome, the Golgi apparatus is a potent MT-organizing organelle. In vivo, scattered Golgi elements stimulate the assembly of noncentrosomal MTs upon recovery from nocodazole treatment.…”

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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%

mentioning

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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“…The coiled-coil TRIP11 protein associates with the minus end of microtubules, which accumulate at the centrosome. 38 Myomegalin has coiled coils such as that found in microtubuleassociated proteins and a leucine zipper identical to that of Drosophila centrosomin. 39 Both TRIP11 and myomegalin are proteins of the Golgi/centrosome region.…”

Section: How Many Mpds Are Centrosomal Diseases?mentioning

confidence: 99%

Myeloproliferative disorders: the centrosome connection

2005

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Some myeloproliferative disorders (MPD) result from a reciprocal translocation that involves the FGFR1 gene and a partner gene. The event creates a chimeric gene that encodes a fusion protein with constitutive FGFR1 tyrosine kinase activity. FGFR1-MPD is a rare disease, but its study may provide interesting clues on different processes such as cell signalling, oncogenesis and stem cell renewal. Some partners of FGFR1 are centrosomal proteins. The corresponding oncogenic fusion kinases are targeted to the centrosome. Constitutive phosphorylation at this site may perturbate centrosome function and the cell cycle. Direct attack at this small organelle may be an efficient way for oncogenes to alter regulation of signalling for proliferation and survival and get rid of checkpoints in cell cycle progression. The same effect might be triggered by other fusion kinases in other MPD and non-MPD malignancies.

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“…Whereas this family was first identified by antibodies from patients with autoimmune diseases, the most characteristic feature of golgins is a large coiledcoil domain similar to that of the myosin family. The golgin family of proteins includes the peripheral membrane proteins GM130 (7), golgin-97 (9), golgin-160 (10,11), golgin-230/245 (12,13), and GMAP-210 (14), as well as the integral membrane proteins golgin-67 (15), golgin-84 (16), and giantin (17).…”

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confidence: 99%

The NH2-terminal Domain of Golgin-160 Contains Both Golgi and Nuclear Targeting Information

Hicks

Machamer

2002

Journal of Biological Chemistry

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Golgin-160 is a member of the golgin family of Golgilocalized membrane proteins. The COOH-terminal twothirds of golgin-160 is predicted to form a coiled-coil, with an NH 2 -terminal "head" domain. To identify the Golgi targeting information in golgin-160, full-length and deletion constructs tagged with green fluorescent protein were generated. The head domain alone was targeted to the Golgi complex in the absence of assembly with endogenous golgin-160. Further truncations from both ends of the head domain narrowed the Golgi targeting information to 85 amino acids between residues 172 and 257. Surprisingly, certain truncations of the head domain also specifically accumulated in the nucleus. Both a nuclear localization signal (masked in the full-length protein) and information for nuclear retention contributed to the nuclear localization of these truncations. Because the golgin-160 head is cleaved by caspases during apoptosis, we examined the localization of epitope-tagged proteins corresponding to all potential caspase cleavage fragments. Our data suggest that three of six fragments could be targeted to the nucleus, provided that they are released from Golgi membranes after cleavage. The finding that both Golgi and nuclear targeting information is present in the same region of golgin-160 suggests that this protein may have more than one function.

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GMAP-210, A Cis-Golgi Network-associated Protein, Is a Minus End Microtubule-binding Protein

Cited by 155 publications

References 60 publications

The Golgi Complex Is a Microtubule-organizing Organelle

The Golgi Complex Is a Microtubule-organizing Organelle

Myeloproliferative disorders: the centrosome connection

The NH2-terminal Domain of Golgin-160 Contains Both Golgi and Nuclear Targeting Information

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