Holliday junction recognition protein (HJURP)

Holliday junction recognition protein (HJURP) is a specialized histone chaperone responsible for the precise deposition of the histone H3 variant CENP-A at centromeres during early G1 phase, a process crucial for the assembly of functional centromeres and proper kinetochore formation[1][2][3]. HJURP interacts directly with CENP-A and histone H4 forming a heterotrimeric complex, and facilitates the expansion of centromeric chromatin by recruiting factors such as the Mis18 complex and CENP-C[1][2]. Structurally, HJURP contains distinct domains mediating its histone chaperone function, centromere localization, and protein-protein interactions[1][2][3]. HJURP is essential for chromosome segregation during cell division and is found predominantly at centromeres and in the nucleolus depending on the cell cycle phase[1]. Abnormal upregulation of HJURP is closely linked to various cancers, where it promotes tumor growth, cell proliferation, and resistance to apoptosis, making it a promising target for cancer therapy and a candidate prognostic biomarker[1].

Other names

Fetal liver-expressing gene 1 proteinFLEG1Up-regulated in lung cancer 9URLC9hFLEG1FAKTS14-3-3-associated AKT substrateDKFZp762E1312SCM3 domain protein (homology to yeast Scm3)

For hypothetical therapeutic targeting: - Inhibition of CENP-A deposition at centromeres (leading to mitotic failure/apoptosis in dividing cells) - Destabilization of kinetochore assembly and chromosome segregation dynamics - Possible modulation of tumor cell proliferation and survival[1][2]