HJURP:CENPA complex localizes to the centromere

Stable Identifier
Reaction [binding]
Homo sapiens
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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
19410545 HJURP is a cell-cycle-dependent maintenance and deposition factor of CENP-A at centromeres

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

Cell 2009
20080577 HJURP binds CENP-A via a highly conserved N-terminal domain and mediates its deposition at centromeres

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

Proc Natl Acad Sci U S A 2010
21768289 HJURP is a CENP-A chromatin assembly factor sufficient to form a functional de novo kinetochore

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

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

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

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

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

Dev Cell 2007
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