title: Two mammalian homologs of yeast Rad23, HR23A and HR23B, as multifunctional proteins.
abstract: Mammalian cells express two homologs of yeast Rad23, the so-called homolog of Rad23 (HR23) proteins. The HR23 proteins were identified more than two decades ago as factors involved in initiation of global genome nucleotide excision repair (GG-NER) along with their interacting partner, xeroderma pigmentosum group C (XPC) protein. Because the HR23 genes encode proteins harboring ubiquitin-like (UBL) domains at their N-termini and two ubiquitin-associated (UBA) domains in their central- and C-terminal regions, the link between HR23 proteins and proteolytic degradation has been widely explored by several methods, including yeast two-hybrid screening and co-affinity purification. To date, various HR23 protein partners have been identified, and these proteins are involved not only in DNA repair, but also in ubiquitin-dependent protein degradation, transcriptional regulation, and cell cycle control. In addition, establishment of mouse strains lacking the HR23 genes and RNA silencing of these genes in human cells demonstrated their significance in animal development and cell growth. Through these studies, the functional differences between the two HR23 proteins have been gradually revealed. Furthermore, recent comprehensive proteomic analyses will help to elucidate the functional protein-protein networks involving the HR23 proteins.
authors: Faculty of Science, Gakushuin University, Toshima-ku, Tokyo 171-8588, Japan; Biosignal Research Center, Kobe University, Kobe, Hyogo 657-8501, Japan.
authors: Masayuki
authors: M
authors: Yokoi
authors: Faculty of Science, Gakushuin University, Toshima-ku, Tokyo 171-8588, Japan; TARA Center, University of Tsukuba, Tsukuba, Ibaraki 305-8577, Japan. Electronic address: fumio.hanaoka@gakushuin.ac.jp.
authors: Fumio
authors: F
authors: Hanaoka
mesh_terms: D000818:Animals; D017209:Apoptosis / Q000502:physiology; D002453:Cell Cycle / Q000235:genetics; D018797:Cell Cycle Proteins / Q000378:metabolism; D049109:Cell Proliferation / Q000502:physiology; D064447:Checkpoint Kinase 2 / Q000378:metabolism; D004260:DNA Repair / Q000502:physiology*; D045643:DNA Repair Enzymes / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D018507:Gene Expression Regulation, Developmental; D006801:Humans; D008322:Mammals; D009369:Neoplasms / Q000235:genetics; D019636:Neurodegenerative Diseases / Q000235:genetics; D055550:Protein Stability; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism
chemical_list: D018797:Cell Cycle Proteins; D004268:DNA-Binding Proteins; C513287:RAD23B protein, human; D029701:Saccharomyces cerevisiae Proteins; C086985:RAD23A protein, human; C086984:XPC protein, human; D064447:Checkpoint Kinase 2; C067022:RAD53 protein, S cerevisiae; D045643:DNA Repair Enzymes
keywords: 26S proteasome; Development; Nucleotide excision repair; Ubiquitin-associated (UBA) domain; Ubiquitin-like (UBL) domain; XPC