Eintrag weiter verarbeiten
The checkpoint protein MAD2 and the mitotic regulator CDC20 form a ternary complex with the anaphase-promoting complex to control anaphase initiation
Gespeichert in:
Zeitschriftentitel: | Genes & Development |
---|---|
Personen und Körperschaften: | , , |
In: | Genes & Development, 12, 1998, 12, S. 1871-1883 |
Format: | E-Article |
Sprache: | Englisch |
veröffentlicht: |
Cold Spring Harbor Laboratory
|
Schlagwörter: |
author_facet |
Fang, Guowei Yu, Hongtao Kirschner, Marc W. Fang, Guowei Yu, Hongtao Kirschner, Marc W. |
---|---|
author |
Fang, Guowei Yu, Hongtao Kirschner, Marc W. |
spellingShingle |
Fang, Guowei Yu, Hongtao Kirschner, Marc W. Genes & Development The checkpoint protein MAD2 and the mitotic regulator CDC20 form a ternary complex with the anaphase-promoting complex to control anaphase initiation Developmental Biology Genetics |
author_sort |
fang, guowei |
spelling |
Fang, Guowei Yu, Hongtao Kirschner, Marc W. 0890-9369 1549-5477 Cold Spring Harbor Laboratory Developmental Biology Genetics http://dx.doi.org/10.1101/gad.12.12.1871 <jats:p>The spindle assembly checkpoint mechanism delays anaphase initiation until all chromosomes are aligned at the metaphase plate. Activation of the anaphase-promoting complex (APC) by binding of CDC20 and CDH1 is required for exit from mitosis, and APC has been implicated as a target for the checkpoint intervention. We show that the human checkpoint protein hMAD2 prevents activation of APC by forming a hMAD2–CDC20–APC complex. When injected into <jats:italic>Xenopus</jats:italic> embryos, hMAD2 arrests cells at mitosis with an inactive APC. The recombinant hMAD2 protein exists in two-folded states: a tetramer and a monomer. Both the tetramer and the monomer bind to CDC20, but only the tetramer inhibits activation of APC and blocks cell cycle progression. Thus, hMAD2 binding is not sufficient for inhibition, and a change in hMAD2 structure may play a role in transducing the checkpoint signal. There are at least three different forms of mitotic APC that can be detected in vivo: an inactive hMAD2–CDC20–APC ternary complex present at metaphase, a CDC20–APC binary complex active in degrading specific substrates at anaphase, and a CDH1–APC complex active later in mitosis and in G<jats:sub>1</jats:sub>. We conclude that the checkpoint-mediated cell cycle arrest involves hMAD2 receiving an upstream signal to inhibit activation of APC.</jats:p> The checkpoint protein MAD2 and the mitotic regulator CDC20 form a ternary complex with the anaphase-promoting complex to control anaphase initiation Genes & Development |
doi_str_mv |
10.1101/gad.12.12.1871 |
facet_avail |
Online Free |
finc_class_facet |
Biologie |
format |
ElectronicArticle |
fullrecord |
blob:ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTEwMS9nYWQuMTIuMTIuMTg3MQ |
id |
ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTEwMS9nYWQuMTIuMTIuMTg3MQ |
institution |
DE-D275 DE-Bn3 DE-Brt1 DE-Zwi2 DE-D161 DE-Gla1 DE-Zi4 DE-15 DE-Pl11 DE-Rs1 DE-105 DE-14 DE-Ch1 DE-L229 |
imprint |
Cold Spring Harbor Laboratory, 1998 |
imprint_str_mv |
Cold Spring Harbor Laboratory, 1998 |
issn |
0890-9369 1549-5477 |
issn_str_mv |
0890-9369 1549-5477 |
language |
English |
mega_collection |
Cold Spring Harbor Laboratory (CrossRef) |
match_str |
fang1998thecheckpointproteinmad2andthemitoticregulatorcdc20formaternarycomplexwiththeanaphasepromotingcomplextocontrolanaphaseinitiation |
publishDateSort |
1998 |
publisher |
Cold Spring Harbor Laboratory |
recordtype |
ai |
record_format |
ai |
series |
Genes & Development |
source_id |
49 |
title |
The checkpoint protein MAD2 and the mitotic regulator CDC20 form a ternary complex with the anaphase-promoting complex to control anaphase initiation |
title_unstemmed |
The checkpoint protein MAD2 and the mitotic regulator CDC20 form a ternary complex with the anaphase-promoting complex to control anaphase initiation |
title_full |
The checkpoint protein MAD2 and the mitotic regulator CDC20 form a ternary complex with the anaphase-promoting complex to control anaphase initiation |
title_fullStr |
The checkpoint protein MAD2 and the mitotic regulator CDC20 form a ternary complex with the anaphase-promoting complex to control anaphase initiation |
title_full_unstemmed |
The checkpoint protein MAD2 and the mitotic regulator CDC20 form a ternary complex with the anaphase-promoting complex to control anaphase initiation |
title_short |
The checkpoint protein MAD2 and the mitotic regulator CDC20 form a ternary complex with the anaphase-promoting complex to control anaphase initiation |
title_sort |
the checkpoint protein mad2 and the mitotic regulator cdc20 form a ternary complex with the anaphase-promoting complex to control anaphase initiation |
topic |
Developmental Biology Genetics |
url |
http://dx.doi.org/10.1101/gad.12.12.1871 |
publishDate |
1998 |
physical |
1871-1883 |
description |
<jats:p>The spindle assembly checkpoint mechanism delays anaphase initiation until all chromosomes are aligned at the metaphase plate. Activation of the anaphase-promoting complex (APC) by binding of CDC20 and CDH1 is required for exit from mitosis, and APC has been implicated as a target for the checkpoint intervention. We show that the human checkpoint protein hMAD2 prevents activation of APC by forming a hMAD2–CDC20–APC complex. When injected into <jats:italic>Xenopus</jats:italic> embryos, hMAD2 arrests cells at mitosis with an inactive APC. The recombinant hMAD2 protein exists in two-folded states: a tetramer and a monomer. Both the tetramer and the monomer bind to CDC20, but only the tetramer inhibits activation of APC and blocks cell cycle progression. Thus, hMAD2 binding is not sufficient for inhibition, and a change in hMAD2 structure may play a role in transducing the checkpoint signal. There are at least three different forms of mitotic APC that can be detected in vivo: an inactive hMAD2–CDC20–APC ternary complex present at metaphase, a CDC20–APC binary complex active in degrading specific substrates at anaphase, and a CDH1–APC complex active later in mitosis and in G<jats:sub>1</jats:sub>. We conclude that the checkpoint-mediated cell cycle arrest involves hMAD2 receiving an upstream signal to inhibit activation of APC.</jats:p> |
container_issue |
12 |
container_start_page |
1871 |
container_title |
Genes & Development |
container_volume |
12 |
format_de105 |
Article, E-Article |
format_de14 |
Article, E-Article |
format_de15 |
Article, E-Article |
format_de520 |
Article, E-Article |
format_de540 |
Article, E-Article |
format_dech1 |
Article, E-Article |
format_ded117 |
Article, E-Article |
format_degla1 |
E-Article |
format_del152 |
Buch |
format_del189 |
Article, E-Article |
format_dezi4 |
Article |
format_dezwi2 |
Article, E-Article |
format_finc |
Article, E-Article |
format_nrw |
Article, E-Article |
_version_ |
1792344276803256327 |
geogr_code |
not assigned |
last_indexed |
2024-03-01T17:04:43.162Z |
geogr_code_person |
not assigned |
openURL |
url_ver=Z39.88-2004&ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fvufind.svn.sourceforge.net%3Agenerator&rft.title=The+checkpoint+protein+MAD2+and+the+mitotic+regulator+CDC20+form+a+ternary+complex+with+the+anaphase-promoting+complex+to+control+anaphase%E2%80%89initiation&rft.date=1998-06-15&genre=article&issn=1549-5477&volume=12&issue=12&spage=1871&epage=1883&pages=1871-1883&jtitle=Genes+%26+Development&atitle=The+checkpoint+protein+MAD2+and+the+mitotic+regulator+CDC20+form+a+ternary+complex+with+the+anaphase-promoting+complex+to+control+anaphase%E2%80%89initiation&aulast=Kirschner&aufirst=Marc+W.&rft_id=info%3Adoi%2F10.1101%2Fgad.12.12.1871&rft.language%5B0%5D=eng |
SOLR | |
_version_ | 1792344276803256327 |
author | Fang, Guowei, Yu, Hongtao, Kirschner, Marc W. |
author_facet | Fang, Guowei, Yu, Hongtao, Kirschner, Marc W., Fang, Guowei, Yu, Hongtao, Kirschner, Marc W. |
author_sort | fang, guowei |
container_issue | 12 |
container_start_page | 1871 |
container_title | Genes & Development |
container_volume | 12 |
description | <jats:p>The spindle assembly checkpoint mechanism delays anaphase initiation until all chromosomes are aligned at the metaphase plate. Activation of the anaphase-promoting complex (APC) by binding of CDC20 and CDH1 is required for exit from mitosis, and APC has been implicated as a target for the checkpoint intervention. We show that the human checkpoint protein hMAD2 prevents activation of APC by forming a hMAD2–CDC20–APC complex. When injected into <jats:italic>Xenopus</jats:italic> embryos, hMAD2 arrests cells at mitosis with an inactive APC. The recombinant hMAD2 protein exists in two-folded states: a tetramer and a monomer. Both the tetramer and the monomer bind to CDC20, but only the tetramer inhibits activation of APC and blocks cell cycle progression. Thus, hMAD2 binding is not sufficient for inhibition, and a change in hMAD2 structure may play a role in transducing the checkpoint signal. There are at least three different forms of mitotic APC that can be detected in vivo: an inactive hMAD2–CDC20–APC ternary complex present at metaphase, a CDC20–APC binary complex active in degrading specific substrates at anaphase, and a CDH1–APC complex active later in mitosis and in G<jats:sub>1</jats:sub>. We conclude that the checkpoint-mediated cell cycle arrest involves hMAD2 receiving an upstream signal to inhibit activation of APC.</jats:p> |
doi_str_mv | 10.1101/gad.12.12.1871 |
facet_avail | Online, Free |
finc_class_facet | Biologie |
format | ElectronicArticle |
format_de105 | Article, E-Article |
format_de14 | Article, E-Article |
format_de15 | Article, E-Article |
format_de520 | Article, E-Article |
format_de540 | Article, E-Article |
format_dech1 | Article, E-Article |
format_ded117 | Article, E-Article |
format_degla1 | E-Article |
format_del152 | Buch |
format_del189 | Article, E-Article |
format_dezi4 | Article |
format_dezwi2 | Article, E-Article |
format_finc | Article, E-Article |
format_nrw | Article, E-Article |
geogr_code | not assigned |
geogr_code_person | not assigned |
id | ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTEwMS9nYWQuMTIuMTIuMTg3MQ |
imprint | Cold Spring Harbor Laboratory, 1998 |
imprint_str_mv | Cold Spring Harbor Laboratory, 1998 |
institution | DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1, DE-L229 |
issn | 0890-9369, 1549-5477 |
issn_str_mv | 0890-9369, 1549-5477 |
language | English |
last_indexed | 2024-03-01T17:04:43.162Z |
match_str | fang1998thecheckpointproteinmad2andthemitoticregulatorcdc20formaternarycomplexwiththeanaphasepromotingcomplextocontrolanaphaseinitiation |
mega_collection | Cold Spring Harbor Laboratory (CrossRef) |
physical | 1871-1883 |
publishDate | 1998 |
publishDateSort | 1998 |
publisher | Cold Spring Harbor Laboratory |
record_format | ai |
recordtype | ai |
series | Genes & Development |
source_id | 49 |
spelling | Fang, Guowei Yu, Hongtao Kirschner, Marc W. 0890-9369 1549-5477 Cold Spring Harbor Laboratory Developmental Biology Genetics http://dx.doi.org/10.1101/gad.12.12.1871 <jats:p>The spindle assembly checkpoint mechanism delays anaphase initiation until all chromosomes are aligned at the metaphase plate. Activation of the anaphase-promoting complex (APC) by binding of CDC20 and CDH1 is required for exit from mitosis, and APC has been implicated as a target for the checkpoint intervention. We show that the human checkpoint protein hMAD2 prevents activation of APC by forming a hMAD2–CDC20–APC complex. When injected into <jats:italic>Xenopus</jats:italic> embryos, hMAD2 arrests cells at mitosis with an inactive APC. The recombinant hMAD2 protein exists in two-folded states: a tetramer and a monomer. Both the tetramer and the monomer bind to CDC20, but only the tetramer inhibits activation of APC and blocks cell cycle progression. Thus, hMAD2 binding is not sufficient for inhibition, and a change in hMAD2 structure may play a role in transducing the checkpoint signal. There are at least three different forms of mitotic APC that can be detected in vivo: an inactive hMAD2–CDC20–APC ternary complex present at metaphase, a CDC20–APC binary complex active in degrading specific substrates at anaphase, and a CDH1–APC complex active later in mitosis and in G<jats:sub>1</jats:sub>. We conclude that the checkpoint-mediated cell cycle arrest involves hMAD2 receiving an upstream signal to inhibit activation of APC.</jats:p> The checkpoint protein MAD2 and the mitotic regulator CDC20 form a ternary complex with the anaphase-promoting complex to control anaphase initiation Genes & Development |
spellingShingle | Fang, Guowei, Yu, Hongtao, Kirschner, Marc W., Genes & Development, The checkpoint protein MAD2 and the mitotic regulator CDC20 form a ternary complex with the anaphase-promoting complex to control anaphase initiation, Developmental Biology, Genetics |
title | The checkpoint protein MAD2 and the mitotic regulator CDC20 form a ternary complex with the anaphase-promoting complex to control anaphase initiation |
title_full | The checkpoint protein MAD2 and the mitotic regulator CDC20 form a ternary complex with the anaphase-promoting complex to control anaphase initiation |
title_fullStr | The checkpoint protein MAD2 and the mitotic regulator CDC20 form a ternary complex with the anaphase-promoting complex to control anaphase initiation |
title_full_unstemmed | The checkpoint protein MAD2 and the mitotic regulator CDC20 form a ternary complex with the anaphase-promoting complex to control anaphase initiation |
title_short | The checkpoint protein MAD2 and the mitotic regulator CDC20 form a ternary complex with the anaphase-promoting complex to control anaphase initiation |
title_sort | the checkpoint protein mad2 and the mitotic regulator cdc20 form a ternary complex with the anaphase-promoting complex to control anaphase initiation |
title_unstemmed | The checkpoint protein MAD2 and the mitotic regulator CDC20 form a ternary complex with the anaphase-promoting complex to control anaphase initiation |
topic | Developmental Biology, Genetics |
url | http://dx.doi.org/10.1101/gad.12.12.1871 |