MozartV1, PascalFrancis, Corpus, bibRecord, 000041

Arabidopsis GCP3-interacting protein 1/MOZART 1 is an integral component of the γ-tubulin-containing microtubule nucleating complex

Identifieur interne : 000041 ( PascalFrancis/Corpus ); précédent : 000040; suivant : 000042

Arabidopsis GCP3-interacting protein 1/MOZART 1 is an integral component of the γ-tubulin-containing microtubule nucleating complex

Auteurs : Masayoshi Nakamura ; Noriyoshi Yagi ; Takehide Kato ; Satoshi Fujita ; Noriyuki Kawashima ; David W. Ehrhardt ; Takashi Hashimoto

Source :

Plant journal [ 0960-7412 ] ; 2012.

RBID : Pascal:12-0300833

Descripteurs français

Pascal (Inist)
- Arabidopsis thaliana, Interaction moléculaire, Tubuline, Microtubule, Complexe, Nucléation.

English descriptors

KwdEn :
- Arabidopsis thaliana, Complexes, Microtubule, Molecular interaction, Nucleation, Tubulin.

Abstract

Microtubules in eukaryotic cells are nucleated from ring-shaped complexes that contain γ-tubulin and a family of homologous γ-tubulin complex proteins (GCPs), but the subunit composition of the complexes can vary among fungi, animals and plants. Arabidopsis GCP3-interacting protein 1 (GIP1), a small protein with no homology to the GCP family, interacts with GCP3 in vitro, and is a plant homolog of vertebrate mitotic-spindle organizing protein associated with a ring of γ-tubulin 1 (MOZART1), a recently identified component of the γ-tubulin complex in human cell lines. In this study, we characterized two closely related Arabidopsis GIP1s: GIP1a and GIP1b. Single mutants of gip1a and gip1b were indistinguishable from wild-type plants, but their double mutant was embryonic lethal, and showed impaired development of male gametophytes. Functional fusions of GIP1a with green fluorescent protein (GFP) were used to purify GIP1a-containing complexes from Arabidopsis plants, which contained all the subunits (except NEDD1) previously identified in the Arabidopsis γ-tubulin complexes. GIP1a and GIP1b interacted specifically with Arabidopsis GCP3 in yeast. GFP-GIP1a labeled mitotic microtubule arrays in a pattern largely consistent with, but partly distinct from, the localization of the γ-tubulin complex containing GCP2 or GCP3 in planta. In interphase cortical arrays, the labeled complexes were preferentially recruited to existing microtubules, from which new microtubules were efficiently nucleated. However, in contrast to complexes labeled with tagged GCP2 or GCP3, their recruitment to cortical areas with no microtubules was rarely observed. These results indicate that GIP1/MOZART1 is an integral component of a subset of the Arabidopsis γ-tubulin complexes.

Notice en format standard (ISO 2709)

Pour connaître la documentation sur le format Inist Standard.

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A03		`1`		`@0 Plant j.`
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A08	`01`	`1`	`ENG`	`@1 Arabidopsis GCP3-interacting protein 1/MOZART 1 is an integral component of the γ-tubulin-containing microtubule nucleating complex`
A11	`01`	`1`		`@1 NAKAMURA (Masayoshi)`
A11	`02`	`1`		`@1 YAGI (Noriyoshi)`
A11	`03`	`1`		`@1 KATO (Takehide)`
A11	`04`	`1`		`@1 FUJITA (Satoshi)`
A11	`05`	`1`		`@1 KAWASHIMA (Noriyuki)`
A11	`06`	`1`		`@1 EHRHARDT (David W.)`
A11	`07`	`1`		`@1 HASHIMOTO (Takashi)`
A14	`01`			`@1 Graduate School of Biological Sciences, Nara Institute of Science and Technology @2 Ikoma, Nara 630-0192 @3 JPN @Z 1 aut. @Z 2 aut. @Z 3 aut. @Z 4 aut. @Z 5 aut. @Z 7 aut.`
A14	`02`			`@1 Department of Plant Biology, Carnegie Institute for Science @2 Stanford, CA 94305 @3 USA @Z 1 aut. @Z 6 aut.`
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A44				`@0 0000 @1 © 2012 INIST-CNRS. All rights reserved.`
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A64	`01`	`1`		`@0 Plant journal`
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C01	`01`		`ENG`	@0 Microtubules in eukaryotic cells are nucleated from ring-shaped complexes that contain γ-tubulin and a family of homologous γ-tubulin complex proteins (GCPs), but the subunit composition of the complexes can vary among fungi, animals and plants. Arabidopsis GCP3-interacting protein 1 (GIP1), a small protein with no homology to the GCP family, interacts with GCP3 in vitro, and is a plant homolog of vertebrate mitotic-spindle organizing protein associated with a ring of γ-tubulin 1 (MOZART1), a recently identified component of the γ-tubulin complex in human cell lines. In this study, we characterized two closely related Arabidopsis GIP1s: GIP1a and GIP1b. Single mutants of gip1a and gip1b were indistinguishable from wild-type plants, but their double mutant was embryonic lethal, and showed impaired development of male gametophytes. Functional fusions of GIP1a with green fluorescent protein (GFP) were used to purify GIP1a-containing complexes from Arabidopsis plants, which contained all the subunits (except NEDD1) previously identified in the Arabidopsis γ-tubulin complexes. GIP1a and GIP1b interacted specifically with Arabidopsis GCP3 in yeast. GFP-GIP1a labeled mitotic microtubule arrays in a pattern largely consistent with, but partly distinct from, the localization of the γ-tubulin complex containing GCP2 or GCP3 in planta. In interphase cortical arrays, the labeled complexes were preferentially recruited to existing microtubules, from which new microtubules were efficiently nucleated. However, in contrast to complexes labeled with tagged GCP2 or GCP3, their recruitment to cortical areas with no microtubules was rarely observed. These results indicate that GIP1/MOZART1 is an integral component of a subset of the Arabidopsis γ-tubulin complexes.
C02	`01`	`X`		`@0 002A10`
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C03	`04`	`X`	`ENG`	`@0 Microtubule @5 04`
C03	`04`	`X`	`SPA`	`@0 Microtúbulo @5 04`
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C03	`05`	`X`	`SPA`	`@0 Complejo @2 NA @5 05`
C03	`06`	`X`	`FRE`	`@0 Nucléation @5 06`
C03	`06`	`X`	`ENG`	`@0 Nucleation @5 06`
C03	`06`	`X`	`SPA`	`@0 Nucleación @5 06`
C07	`01`	`X`	`FRE`	`@0 Cruciferae @2 NS`
C07	`01`	`X`	`ENG`	`@0 Cruciferae @2 NS`
C07	`01`	`X`	`SPA`	`@0 Cruciferae @2 NS`
C07	`02`	`X`	`FRE`	`@0 Dicotyledones @2 NS`
C07	`02`	`X`	`ENG`	`@0 Dicotyledones @2 NS`
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Format Inist (serveur)

NO :	PASCAL 12-0300833 INIST
ET :	Arabidopsis GCP3-interacting protein 1/MOZART 1 is an integral component of the γ-tubulin-containing microtubule nucleating complex
AU :	NAKAMURA (Masayoshi); YAGI (Noriyoshi); KATO (Takehide); FUJITA (Satoshi); KAWASHIMA (Noriyuki); EHRHARDT (David W.); HASHIMOTO (Takashi)
AF :	Graduate School of Biological Sciences, Nara Institute of Science and Technology/Ikoma, Nara 630-0192/Japon (1 aut., 2 aut., 3 aut., 4 aut., 5 aut., 7 aut.); Department of Plant Biology, Carnegie Institute for Science/Stanford, CA 94305/Etats-Unis (1 aut., 6 aut.)
DT :	Publication en série; Niveau analytique
SO :	Plant journal; ISSN 0960-7412; Royaume-Uni; Da. 2012; Vol. 71; No. 2; Pp. 216-225; Bibl. 3/4 p.
LA :	Anglais
EA :	Microtubules in eukaryotic cells are nucleated from ring-shaped complexes that contain γ-tubulin and a family of homologous γ-tubulin complex proteins (GCPs), but the subunit composition of the complexes can vary among fungi, animals and plants. Arabidopsis GCP3-interacting protein 1 (GIP1), a small protein with no homology to the GCP family, interacts with GCP3 in vitro, and is a plant homolog of vertebrate mitotic-spindle organizing protein associated with a ring of γ-tubulin 1 (MOZART1), a recently identified component of the γ-tubulin complex in human cell lines. In this study, we characterized two closely related Arabidopsis GIP1s: GIP1a and GIP1b. Single mutants of gip1a and gip1b were indistinguishable from wild-type plants, but their double mutant was embryonic lethal, and showed impaired development of male gametophytes. Functional fusions of GIP1a with green fluorescent protein (GFP) were used to purify GIP1a-containing complexes from Arabidopsis plants, which contained all the subunits (except NEDD1) previously identified in the Arabidopsis γ-tubulin complexes. GIP1a and GIP1b interacted specifically with Arabidopsis GCP3 in yeast. GFP-GIP1a labeled mitotic microtubule arrays in a pattern largely consistent with, but partly distinct from, the localization of the γ-tubulin complex containing GCP2 or GCP3 in planta. In interphase cortical arrays, the labeled complexes were preferentially recruited to existing microtubules, from which new microtubules were efficiently nucleated. However, in contrast to complexes labeled with tagged GCP2 or GCP3, their recruitment to cortical areas with no microtubules was rarely observed. These results indicate that GIP1/MOZART1 is an integral component of a subset of the Arabidopsis γ-tubulin complexes.
CC :	002A10; 002A03H01
FD :	Arabidopsis thaliana; Interaction moléculaire; Tubuline; Microtubule; Complexe; Nucléation
FG :	Cruciferae; Dicotyledones; Angiospermae; Spermatophyta
ED :	Arabidopsis thaliana; Molecular interaction; Tubulin; Microtubule; Complexes; Nucleation
EG :	Cruciferae; Dicotyledones; Angiospermae; Spermatophyta
SD :	Arabidopsis thaliana; Interacción molecular; Tubulina; Microtúbulo; Complejo; Nucleación
LO :	INIST-26050.354000500844000040
ID :	12-0300833

Links to Exploration step

Pascal:12-0300833

Le document en format XML

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<front><div type="abstract" xml:lang="en">Microtubules in eukaryotic cells are nucleated from ring-shaped complexes that contain γ-tubulin and a family of homologous γ-tubulin complex proteins (GCPs), but the subunit composition of the complexes can vary among fungi, animals and plants. Arabidopsis GCP3-interacting protein 1 (GIP1), a small protein with no homology to the GCP family, interacts with GCP3 in vitro, and is a plant homolog of vertebrate mitotic-spindle organizing protein associated with a ring of γ-tubulin 1 (MOZART1), a recently identified component of the γ-tubulin complex in human cell lines. In this study, we characterized two closely related Arabidopsis GIP1s: GIP1a and GIP1b. Single mutants of gip1a and gip1b were indistinguishable from wild-type plants, but their double mutant was embryonic lethal, and showed impaired development of male gametophytes. Functional fusions of GIP1a with green fluorescent protein (GFP) were used to purify GIP1a-containing complexes from Arabidopsis plants, which contained all the subunits (except NEDD1) previously identified in the Arabidopsis γ-tubulin complexes. GIP1a and GIP1b interacted specifically with Arabidopsis GCP3 in yeast. GFP-GIP1a labeled mitotic microtubule arrays in a pattern largely consistent with, but partly distinct from, the localization of the γ-tubulin complex containing GCP2 or GCP3 in planta. In interphase cortical arrays, the labeled complexes were preferentially recruited to existing microtubules, from which new microtubules were efficiently nucleated. However, in contrast to complexes labeled with tagged GCP2 or GCP3, their recruitment to cortical areas with no microtubules was rarely observed. These results indicate that GIP1/MOZART1 is an integral component of a subset of the Arabidopsis γ-tubulin complexes.</div>
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<fA14 i1="01"><s1>Graduate School of Biological Sciences, Nara Institute of Science and Technology</s1>
<s2>Ikoma, Nara 630-0192</s2>
<s3>JPN</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>4 aut.</sZ>
<sZ>5 aut.</sZ>
<sZ>7 aut.</sZ>
</fA14>
<fA14 i1="02"><s1>Department of Plant Biology, Carnegie Institute for Science</s1>
<s2>Stanford, CA 94305</s2>
<s3>USA</s3>
<sZ>1 aut.</sZ>
<sZ>6 aut.</sZ>
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<fA20><s1>216-225</s1>
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<fA21><s1>2012</s1>
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<fA47 i1="01" i2="1"><s0>12-0300833</s0>
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<fA60><s1>P</s1>
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<fA61><s0>A</s0>
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<fA64 i1="01" i2="1"><s0>Plant journal</s0>
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<fA66 i1="01"><s0>GBR</s0>
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<fC01 i1="01" l="ENG"><s0>Microtubules in eukaryotic cells are nucleated from ring-shaped complexes that contain γ-tubulin and a family of homologous γ-tubulin complex proteins (GCPs), but the subunit composition of the complexes can vary among fungi, animals and plants. Arabidopsis GCP3-interacting protein 1 (GIP1), a small protein with no homology to the GCP family, interacts with GCP3 in vitro, and is a plant homolog of vertebrate mitotic-spindle organizing protein associated with a ring of γ-tubulin 1 (MOZART1), a recently identified component of the γ-tubulin complex in human cell lines. In this study, we characterized two closely related Arabidopsis GIP1s: GIP1a and GIP1b. Single mutants of gip1a and gip1b were indistinguishable from wild-type plants, but their double mutant was embryonic lethal, and showed impaired development of male gametophytes. Functional fusions of GIP1a with green fluorescent protein (GFP) were used to purify GIP1a-containing complexes from Arabidopsis plants, which contained all the subunits (except NEDD1) previously identified in the Arabidopsis γ-tubulin complexes. GIP1a and GIP1b interacted specifically with Arabidopsis GCP3 in yeast. GFP-GIP1a labeled mitotic microtubule arrays in a pattern largely consistent with, but partly distinct from, the localization of the γ-tubulin complex containing GCP2 or GCP3 in planta. In interphase cortical arrays, the labeled complexes were preferentially recruited to existing microtubules, from which new microtubules were efficiently nucleated. However, in contrast to complexes labeled with tagged GCP2 or GCP3, their recruitment to cortical areas with no microtubules was rarely observed. These results indicate that GIP1/MOZART1 is an integral component of a subset of the Arabidopsis γ-tubulin complexes.</s0>
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<s5>03</s5>
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<s5>03</s5>
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<s5>04</s5>
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<s5>04</s5>
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<s5>04</s5>
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<s2>NA</s2>
<s5>05</s5>
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<s2>NA</s2>
<s5>05</s5>
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<s2>NA</s2>
<s5>05</s5>
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<s5>06</s5>
</fC03>
<fC03 i1="06" i2="X" l="SPA"><s0>Nucleación</s0>
<s5>06</s5>
</fC03>
<fC07 i1="01" i2="X" l="FRE"><s0>Cruciferae</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="01" i2="X" l="ENG"><s0>Cruciferae</s0>
<s2>NS</s2>
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<s2>NS</s2>
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<s2>NS</s2>
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<fC07 i1="02" i2="X" l="ENG"><s0>Dicotyledones</s0>
<s2>NS</s2>
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<s2>NS</s2>
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<fC07 i1="03" i2="X" l="FRE"><s0>Angiospermae</s0>
<s2>NS</s2>
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<s2>NS</s2>
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<s2>NS</s2>
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<fC07 i1="04" i2="X" l="FRE"><s0>Spermatophyta</s0>
<s2>NS</s2>
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<fC07 i1="04" i2="X" l="ENG"><s0>Spermatophyta</s0>
<s2>NS</s2>
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<fC07 i1="04" i2="X" l="SPA"><s0>Spermatophyta</s0>
<s2>NS</s2>
</fC07>
<fN21><s1>226</s1>
</fN21>
<fN44 i1="01"><s1>OTO</s1>
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<fN82><s1>OTO</s1>
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<server><NO>PASCAL 12-0300833 INIST</NO>
<ET>Arabidopsis GCP3-interacting protein 1/MOZART 1 is an integral component of the γ-tubulin-containing microtubule nucleating complex</ET>
<AU>NAKAMURA (Masayoshi); YAGI (Noriyoshi); KATO (Takehide); FUJITA (Satoshi); KAWASHIMA (Noriyuki); EHRHARDT (David W.); HASHIMOTO (Takashi)</AU>
<AF>Graduate School of Biological Sciences, Nara Institute of Science and Technology/Ikoma, Nara 630-0192/Japon (1 aut., 2 aut., 3 aut., 4 aut., 5 aut., 7 aut.); Department of Plant Biology, Carnegie Institute for Science/Stanford, CA 94305/Etats-Unis (1 aut., 6 aut.)</AF>
<DT>Publication en série; Niveau analytique</DT>
<SO>Plant journal; ISSN 0960-7412; Royaume-Uni; Da. 2012; Vol. 71; No. 2; Pp. 216-225; Bibl. 3/4 p.</SO>
<LA>Anglais</LA>
<EA>Microtubules in eukaryotic cells are nucleated from ring-shaped complexes that contain γ-tubulin and a family of homologous γ-tubulin complex proteins (GCPs), but the subunit composition of the complexes can vary among fungi, animals and plants. Arabidopsis GCP3-interacting protein 1 (GIP1), a small protein with no homology to the GCP family, interacts with GCP3 in vitro, and is a plant homolog of vertebrate mitotic-spindle organizing protein associated with a ring of γ-tubulin 1 (MOZART1), a recently identified component of the γ-tubulin complex in human cell lines. In this study, we characterized two closely related Arabidopsis GIP1s: GIP1a and GIP1b. Single mutants of gip1a and gip1b were indistinguishable from wild-type plants, but their double mutant was embryonic lethal, and showed impaired development of male gametophytes. Functional fusions of GIP1a with green fluorescent protein (GFP) were used to purify GIP1a-containing complexes from Arabidopsis plants, which contained all the subunits (except NEDD1) previously identified in the Arabidopsis γ-tubulin complexes. GIP1a and GIP1b interacted specifically with Arabidopsis GCP3 in yeast. GFP-GIP1a labeled mitotic microtubule arrays in a pattern largely consistent with, but partly distinct from, the localization of the γ-tubulin complex containing GCP2 or GCP3 in planta. In interphase cortical arrays, the labeled complexes were preferentially recruited to existing microtubules, from which new microtubules were efficiently nucleated. However, in contrast to complexes labeled with tagged GCP2 or GCP3, their recruitment to cortical areas with no microtubules was rarely observed. These results indicate that GIP1/MOZART1 is an integral component of a subset of the Arabidopsis γ-tubulin complexes.</EA>
<CC>002A10; 002A03H01</CC>
<FD>Arabidopsis thaliana; Interaction moléculaire; Tubuline; Microtubule; Complexe; Nucléation</FD>
<FG>Cruciferae; Dicotyledones; Angiospermae; Spermatophyta</FG>
<ED>Arabidopsis thaliana; Molecular interaction; Tubulin; Microtubule; Complexes; Nucleation</ED>
<EG>Cruciferae; Dicotyledones; Angiospermae; Spermatophyta</EG>
<SD>Arabidopsis thaliana; Interacción molecular; Tubulina; Microtúbulo; Complejo; Nucleación</SD>
<LO>INIST-26050.354000500844000040</LO>
<ID>12-0300833</ID>
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Arabidopsis GCP3-interacting protein 1/MOZART 1 is an integral component of the γ-tubulin-containing microtubule nucleating complex

Arabidopsis GCP3-interacting protein 1/MOZART 1 is an integral component of the γ-tubulin-containing microtubule nucleating complex

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