Posttranslational Glutamylation of α-tubulin

Eddé, Bernard; Rossier, Jean; Caer, JP Le; Desbruyères, E.; Gros, François; Denoulet, Philippe

doi:10.1126/science.1967194

Cited by 511 publications

(442 citation statements)

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“…Consistently, neither was polyglutamylated tubulin (Eddé et al, 1990) detected in Golgi samples (our unpublished results). To evaluate from Figure 7B the specificity of ␥-tubulin binding to Golgi membranes, a ␥-tubulin to centrin ratio was measured in the Golgi and in the nucleo-centrosomal extract.…”

Section: ␥-Tubulin Is Involved In the Nucleation Of Golgibased Mtssupporting

confidence: 56%

“…Various markers of the Golgi were used including an mAb to rat mannosidase II (clone 53FC3) from Berkeley Antibody Co. (Richmond, CA), antialbumin immunserum raised in rabbits as previously described (Biou et al 1984), anti-GM130 Golgi matrix protein (Transduction Laboratories, Lexington, KY), and anti-TGN38, kindly provided by Dr. George Banting, Department of Biochemistry, School of Medical Sciences, University of Bristol, UK (Reaves and Banting, 1992). For the detection of centriolar proteins, we used the mAb (clone GT335) to polyglutamylated tubulin (Eddé et al, 1990), kindly provided by Pr. Philippe Denoulet (Centre National de la Recherche Scientifique, FRE2219 Université Paris VI) and a polyclonal antibody to centrin-3 (Middendorp et al, 1997), kindly provided by Dr. Michel Bornens (Centre National de la Recherche Scientifique, Unité Mixte de Recherche 144, Institut Curie, Paris), who also provided the nucleo-centrosomal extract used as a positive control.…”

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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

275

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: ␥-Tubulin Is Involved In the Nucleation Of Golgibased Mtssupporting

confidence: 56%

mentioning

confidence: 99%

The Golgi Complex Is a Microtubule-organizing Organelle

Chabin-Brion

Marceiller

Perez

et al. 2001

MBoC

275

245

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“…It has been long known that tubulin undergoes acetylation that correlates with microtubule stability and microtubule-based organelle transport (Bulinski, 2007;Reed et al, 2006), which is important for the delivery of membranous components for cell polarization and protrusion to the cell leading edge. Tubulin is also modified by post-translational phosphorylation and detyrosynation, as well as addition of tyrosine (Raybin and Flavin, 1977a;b), mono-and poly-glutamine (Audebert et al, 1993;Edde et al, 1990), and glycine (Plessmann and Weber, 1997) (see also (Luduena, 1998) for an overview of tubulin modifications). Some of these tubulin modifications have been associated with microtubule stability and found to serve as markers for cell polarization (Erck et al, 2005;Gundersen and Bulinski, 1986;Infante et al, 2000;Khawaja et al, 1988).…”

Section: Posttranslational Regulation Of Cell Migrationmentioning

confidence: 99%

Cell biology of embryonic migration

Kurosaka¹,

Kashina²

2008

Birth Defects Research Pt C

113

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Cell migration is an evolutionarily conserved mechanism that underlies the development and functioning of uni-and multicellular organisms and takes place in normal and pathogenic processes, including various events of embryogenesis, wound healing, immune response, cancer metastases, and angiogenesis. Despite the differences in the cell types that take part in different migratory events, it is believed that all of these migrations occur by similar molecular mechanisms, whose major components have been functionally conserved in evolution and whose perturbation leads to severe developmental defects. These mechanisms involve intricate cytoskeleton-based molecular machines that can sense the environment, respond to signals, and modulate the entire cell behavior. A big question that has concerned the researchers for decades relates to the coordination of cell migration in situ and its relation to the intracellular aspects of the cell migratory mechanisms. Traditionally, this question has been addressed by researchers that considered the intra-and extracellular mechanisms driving migration in separate sets of studies. As more data accumulate researchers are now able to integrate all of the available information and consider the intracellular mechanisms of cell migration in the context of the developing organisms that contain additional levels of complexity provided by extracellular regulation. This review provides a broad summary of the existing and emerging data in the cell and developmental biology fields regarding cell migration during development.

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“…Many PTMs involve the reversible addition of a range of molecules of variable size that range from methyl, phosphate, and acetyl groups, to lipids and small proteins. Glutamylation [1] and glycylation [2] are unusual PTMs, as the amino acids are added as homopolymeric chains of differing length that are covalently attached to a side-chain carboxyl group of individual glutamic acid residues near the carboxyl terminus of specific proteins. These modifications were originally discovered in tubulins.…”

Section: Introductionmentioning

confidence: 99%

TTLL10 is a protein polyglycylase that can modify nucleosome assembly protein 1

et al. 2008

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Certain proteins can undergo polyglycylation and polyglutamylation. Polyglutamylases (glutamate ligases) have recently been identified in a family of tubulin tyrosine ligase-like (TTLL) proteins. However, no polyglycylase (glycine ligase) has yet been reported. Here we identify a polyglycylase in the TTLL proteins by using an anti-poly-glycine antibody. The antibody reacted with a cytoplasmic 60-kDa protein that accumulated in elongating spermatids. Using tandem mass spectrometry of trypsinized samples, immunoprecipitated by the antibody from the TTLL10-expressing cells, we identified the 60-kDa protein as nucleosome assembly protein 1 (NAP1). Recombinant TTLL10 incorporated glycine into recombinant NAP1 in vitro. Mutational analyses indicated that Glu residues at 359 and 360 in the C-terminal part of NAP1 are putative sites for the modification. Thus, TTLL10 is a polyglycylase for NAP1.

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Posttranslational Glutamylation of α-tubulin

Cited by 511 publications

References 15 publications

The Golgi Complex Is a Microtubule-organizing Organelle

The Golgi Complex Is a Microtubule-organizing Organelle

Cell biology of embryonic migration

TTLL10 is a protein polyglycylase that can modify nucleosome assembly protein 1

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