Publication Date:
1998-03-21
Description:
The anaphase-promoting complex is composed of eight protein subunits, including BimE (APC1), CDC27 (APC3), CDC16 (APC6), and CDC23 (APC8). The remaining four human APC subunits, APC2, APC4, APC5, and APC7, as well as human CDC23, were cloned. APC7 contains multiple copies of the tetratrico peptide repeat, similar to CDC16, CDC23, and CDC27. Whereas APC4 and APC5 share no similarity to proteins of known function, APC2 contains a region that is similar to a sequence in cullins, a family of proteins implicated in the ubiquitination of G1 phase cyclins and cyclin-dependent kinase inhibitors. The APC2 gene is essential in Saccharomyces cerevisiae, and apc2 mutants arrest at metaphase and are defective in the degradation of Pds1p. APC2 and cullins may be distantly related members of a ubiquitin ligase family that targets cell cycle regulators for degradation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yu, H -- Peters, J M -- King, R W -- Page, A M -- Hieter, P -- Kirschner, M W -- CA16519/CA/NCI NIH HHS/ -- GM26875-17/GM/NIGMS NIH HHS/ -- GM39023-08/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Feb 20;279(5354):1219-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9469815" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
*Anaphase
;
Anaphase-Promoting Complex-Cyclosome
;
Animals
;
Apc1 Subunit, Anaphase-Promoting Complex-Cyclosome
;
Apc2 Subunit, Anaphase-Promoting Complex-Cyclosome
;
Apc4 Subunit, Anaphase-Promoting Complex-Cyclosome
;
Apc5 Subunit, Anaphase-Promoting Complex-Cyclosome
;
Apc7 Subunit, Anaphase-Promoting Complex-Cyclosome
;
Apc8 Subunit, Anaphase-Promoting Complex-Cyclosome
;
Cell Cycle/*physiology
;
Cell Cycle Proteins/chemistry
;
Cloning, Molecular
;
*Cullin Proteins
;
Helminth Proteins/chemistry
;
Humans
;
Ligases/*chemistry/genetics/metabolism
;
Molecular Sequence Data
;
Mutation
;
Open Reading Frames
;
Phylogeny
;
Proteins/chemistry
;
Saccharomyces cerevisiae/chemistry/cytology/genetics
;
*Saccharomyces cerevisiae Proteins
;
Sequence Alignment
;
*Ubiquitin-Protein Ligase Complexes
;
Ubiquitin-Protein Ligases
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
