HJURP:CENPA complex localizes to the centromere

Stable Identifier
R-HSA-606326
Type
Reaction [binding]
Species
Homo sapiens
Compartment
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The HJURP complex binds free, newly synthesized CENPA-H4 tetramers. A direct interaction occurs between HJURP and CENPA. The CATD domain of CENPA is sufficient for the interaction. The complex then localizes to the centromere in early G1 phase. HJURP is required for deposition of new CENPA-containing nucleosomes.

Literature References
PubMed ID Title Journal Year
20080577 HJURP binds CENP-A via a highly conserved N-terminal domain and mediates its deposition at centromeres

Shuaib, M, Ouararhni, K, Dimitrov, S, Hamiche, A

Proc Natl Acad Sci U S A 2010
19410545 HJURP is a cell-cycle-dependent maintenance and deposition factor of CENP-A at centromeres

Dunleavy, EM, Roche, D, Tagami, H, Lacoste, N, Ray-Gallet, D, Nakamura, Y, Daigo, Y, Nakatani, Y, Almouzni-Pettinotti, G

Cell 2009
21768289 HJURP is a CENP-A chromatin assembly factor sufficient to form a functional de novo kinetochore

Barnhart, MC, Kuich, PH, Stellfox, ME, Ward, JA, Bassett, EA, Black, BE, Foltz, DR

J. Cell Biol. 2011
19410544 Centromere-specific assembly of CENP-a nucleosomes is mediated by HJURP

Foltz, DR, Jansen, LE, Bailey, AO, Yates, JR 3rd, Bassett, EA, Wood, S, Black, BE, Cleveland, DW

Cell 2009
17199038 Priming of centromere for CENP-A recruitment by human hMis18alpha, hMis18beta, and M18BP1

Fujita, Y, Hayashi, T, Kiyomitsu, T, Toyoda, Y, Kokubu, A, Obuse, C, Yanagida, M

Dev Cell 2007
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