Interaction of microtubule-associated proteins with microtubules: yeast lysyl- and valyl-tRNA synthetases and .tau. 218-235 synthetic peptide as model systems

Melki, Ronald; Kerjan, Pierre; Jp, Waller; Mf, Carlier; Pantaloni, Dominique

doi:10.1021/bi00113a008

Cited by 64 publications

(47 citation statements)

References 48 publications

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“…7A shows that when increasing amounts of recombinant rice MFP were added to a constant amount of microtubules (5 M tubulin), binding was saturated at an MFP concentration of ϳ5 M, indicating that the MFP-tubulin interaction was stoichiometric. Although not common, stoichiometric binding of MAPs to tubulin has been reported previously (51,52). This stoichiomet- ric binding for rice MFP and microtubules was also observed when microtubules were assembled from tubulin that was preincubated with MFP (data not shown).…”

Section: Figsupporting

confidence: 74%

Identification of a Rice RNA- and Microtubule-binding Protein as the Multifunctional Protein, a Peroxisomal Enzyme Involved in the β-Oxidation of Fatty Acids

Chuong¹,

Mullen²,

Muench³

2002

Journal of Biological Chemistry

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The control of subcellular mRNA localization and translation is often mediated by protein factors that are directly or indirectly associated with the cytoskeleton. We report the identification and characterization of a rice seed protein that possesses both RNA and microtubule binding activities. In vitro UV cross-linking assays indicated that this protein binds to all mRNA sequences tested, although there was evidence for preferential binding to RNAs that contained A-C nucleotide sequence motifs. The protein was purified to homogeneity using a two-step procedure, and amino acid sequencing identified it as the multifunctional protein (MFP), a peroxisomal enzyme known to possess a number of activities involved in the ␤-oxidation of fatty acids. The recombinant version of this rice MFP binds to RNA in UV cross-linking and gel mobility shift experiments, co-sediments specifically with microtubules, and possesses at least two enzymatic activities involved in peroxisomal fatty acid ␤-oxidation. Taken together these data suggest that MFP has an important role in mRNA physiology in the cytoplasm, perhaps in regulating the localization or translation of mRNAs through an interaction with microtubules, in addition to its peroxisomal function.

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Section: Figsupporting

confidence: 74%

Identification of a Rice RNA- and Microtubule-binding Protein as the Multifunctional Protein, a Peroxisomal Enzyme Involved in the β-Oxidation of Fatty Acids

Chuong¹,

Mullen²,

Muench³

2002

Journal of Biological Chemistry

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“…The remaining tissue was minced in a meat grinder and then homogenized in a Waring blender for 7626 WALDEN AND COWAN cycled calf brain microtubule protein was prepared in a similar manner. Coassembly of calf brain microtubules and in vitro-translated polypeptides was performed as described previously (27). Sedimentation of microtubules through sucrose cushions was carried out according to the method of Melki et al (33). For in vitro kinase assays, microtubules were prepared from 20 g of tissue as described above but with the inclusion of the phosphatase inhibitors Na3VO4 (200 ,uM), NaF (20 mM), and sodium PPi (10 mM).…”

Section: Methodsmentioning

confidence: 99%

A novel 205-kilodalton testis-specific serine/threonine protein kinase associated with microtubules of the spermatid manchette.

Walden¹,

Cowan²

1993

Mol. Cell. Biol.

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To identify proteins which interact with and potentially modulate the function of microtubules during spermatogenesis, we prepared a total testis MAP (microtubule-associated protein) antiserum and used it to isolate cDNA clones from a mouse testis cDNA expression library. Antibodies affinity purified by using one expression clone The process of cellular differentiation is intricately linked to morphological changes in the microtubular cytoskeleton. Microtubules, which form by self-assembly of a-and 3-tubulin heterodimers, require specific interactions with various proteins to establish diverse conformations and to perform their different functions. These interacting proteins are referred to as microtubule-associated proteins (MAPs). Two mechanisms can be envisaged for the involvement of MAPs in microtubule morphogenesis. First, the programmed expression of MAPs may be required for the terminal differentiation of a cell type; examples include MAP2 and tau in the determination of neuronal morphology (7). Second, the signal transduction pathway may influence microtubule organization via phosphorylation of tubulin and/or MAPs. Some kinases have been shown to colocalize with microtubules in vivo, providing a means for rapid phosphorylation of specific microtubule proteins. The c-mos product, which binds and phosphorylates tubulin (48), is an active component of the cytostatic factor, a factor isolated from mature Xenopus oocytes and thought to be responsible for the arrest of fertilized eggs at meiotic metaphase II (31). Among MAPs, phosphorylation of MAP2 has been extensively studied. Phosphorylation of MAP2 reduces its ability to stimulate tubulin assembly in vitro (20,35) and decreases its affinity for microtubules both in vitro (4) and in vivo (3). Type II cyclic AMP (cAMP)-dependent protein kinase phosphorylates and copurifies with brain MAP2 because of the high-affinity binding of RII to the amino terminus of the MAP2 molecule (38,44,45).Mammalian spermatogenesis is a continuum of cellular differentiation that has three principal phases: the mitotic proliferation and renewal of spermatogonia, the meiotic * Corresponding author. Electronic mail address: walden@ mcclbO.med.nyu.edu. divisions of spermatocytes, and spermiogenesis, a complex metamorphosis of the haploid germ cell culminating in the release of late spermatids into the lumen of the seminiferous tubule. During spermatogenesis the microtubular cytoskeleton exists in diverse conformations, including two microtubular arrays unique to spermiogenesis, namely the spermatid manchette and flagellum. The manchette temporally forms around the caudal nucleus of round spermatids and has been implicated in the subsequent process of sperm head shaping (9,32,39).We sought to identify proteins which interact with, and potentially modulate the function of, microtubules during spermatogenesis. We describe here the identification and characterization of one such protein, a novel 205-kDa microtubule-associated serine/threonine protein kinase, termed MAST205. MAST205 col...

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“…Biochemical and structural studies concerning interaction of tau with MTs are typically performed in the presence of the MT-stabilizing drug taxol (Gustke et al, 1994;Littauer et al, 1986;Melki et al, 1991). Recent studies have demonstrated that in the presence of taxol, the dynamics of association of ensconsin (E-MAP-115) with MTs is slowed down by an order of magnitude (Bulinski et al, 2001).…”

Section: Taxol Induces Rapid Detachment Of Tau From Single Mtsmentioning

confidence: 99%

Tau interaction with microtubules in vivo

Samsonov

Rasenick

et al. 2004

Journal of Cell Science

127

102

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Tau is a major microtubule-associated protein which induces bundling and stabilization of axonal microtubules (MTs). To investigate the interaction of tau with MTs in living cells, we expressed GFP-tau fusion protein in cultured Xenopus embryo neurons and performed time-lapse imaging of tau-labeled MTs. Tau uniformly labeled individual MTs regardless of their assembly/disassembly status and location along the axon. Photobleaching experiments indicated that interaction of tau with MTs is very dynamic, with a half-time of fluorescence recovery of the order of 3 seconds. Treatment of cells with taxol, a drug that suppresses MT dynamics, rapidly induced detachment of tau from MTs. Although binding of tau to straight MTs was uniform, there was a heightened concentration of tau at the sites of high MT curvature. Our results suggest that dynamic interaction of tau with MTs may modify local mechanical properties of individual MTs and play a crucial role in the remodeling of the MT cytoskeleton during neuronal plasticity.

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Interaction of microtubule-associated proteins with microtubules: yeast lysyl- and valyl-tRNA synthetases and .tau. 218-235 synthetic peptide as model systems

Cited by 64 publications

References 48 publications

Identification of a Rice RNA- and Microtubule-binding Protein as the Multifunctional Protein, a Peroxisomal Enzyme Involved in the β-Oxidation of Fatty Acids

Identification of a Rice RNA- and Microtubule-binding Protein as the Multifunctional Protein, a Peroxisomal Enzyme Involved in the β-Oxidation of Fatty Acids

A novel 205-kilodalton testis-specific serine/threonine protein kinase associated with microtubules of the spermatid manchette.

Tau interaction with microtubules in vivo

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