title: Ub-family modifications at the replication fork: Regulating PCNA-interacting components.
abstract: A vast array of proteins is recruited to the replication fork in a dynamic and coordinated manner through physical interactions with Proliferating Cell Nuclear Antigen, PCNA. How this complex exchange of PCNA binding partners is choreographed to ensure proper replication origin licensing, DNA synthesis during normal replication or repair of DNA damage, chromatin assembly, DNA methylation, histone modification, and sister chromatid cohesion is only beginning to be appreciated. In this review, several roles of ubiquitin-related modifications in the recruitment and turnover of PCNA-interacting proteins at the replication fork are considered.
authors.affiliation: Department of Biochemistry and Purdue University Center for Cancer Research, Purdue University, 175 S. University St., West Lafayette, IN 47907, USA. kirchmaier@purdue.edu
authors.forename: Ann L
authors.initials: AL
authors.lastname: Kirchmaier
mesh_terms: D000818:Animals; D018797:Cell Cycle Proteins / Q000378:metabolism; D004249:DNA Damage; D004260:DNA Repair; D004261:DNA Replication; D006801:Humans; D009687:Nuclear Proteins / Q000378:metabolism; D018809:Proliferating Cell Nuclear Antigen / Q000378:metabolism*; D011485:Protein Binding; D011499:Protein Processing, Post-Translational; D025801:Ubiquitin / Q000378:metabolism*; D044767:Ubiquitin-Protein Ligases / Q000378:metabolism
chemical_list: C467199:CDT1 protein, human; D018797:Cell Cycle Proteins; C429530:DTL protein, human; D009687:Nuclear Proteins; D018809:Proliferating Cell Nuclear Antigen; D025801:Ubiquitin; D044767:Ubiquitin-Protein Ligases