WRNIP1 accumulates at laser light irradiated sites rapidly via its ubiquitin-binding zinc finger domain and independently from its ATPase domain
► WRNIP1 accumulates in laser light irradiated sites very rapidly via UBZ domain. ► The ATPase domain of WRNIP1 is dispensable for its accumulation. ► The accumulation of WRNIP1 seems not to be dependent on the interaction with WRN. WRNIP1 (Werner helicase-interacting protein 1) was originally ident...
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| Veröffentlicht in: | Biochemical and biophysical research communications 2012-01, Vol.417 (4), p.1145-1150 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Nomura, Hironoshin Yoshimura, Akari Edo, Takato Kanno, Shin-ichiro Tada, Syusuke Seki, Masayuki Yasui, Akira Enomoto, Takemi |
| description | ► WRNIP1 accumulates in laser light irradiated sites very rapidly via UBZ domain. ► The ATPase domain of WRNIP1 is dispensable for its accumulation. ► The accumulation of WRNIP1 seems not to be dependent on the interaction with WRN.
WRNIP1 (Werner helicase-interacting protein 1) was originally identified as a protein that interacts with the Werner syndrome responsible gene product. WRNIP1 contains a ubiquitin-binding zinc-finger (UBZ) domain in the N-terminal region and two leucine zipper motifs in the C-terminal region. In addition, it possesses an ATPase domain in the middle of the molecule and the lysine residues serving as ubiquitin acceptors in the entire of the molecule. Here, we report that WRNIP1 accumulates in laser light irradiated sites very rapidly via its ubiquitin-binding zinc finger domain, which is known to bind polyubiquitin and to be involved in ubiquitination of WRNIP1 itself. The accumulation of WRNIP1 in laser light irradiated sites also required the C-terminal region containing two leucine zippers, which is reportedly involved in the oligomerization of WRNIP1. Mutated WRNIP1 with a deleted ATPase domain or with mutations in lysine residues, which serve as ubiquitin acceptors, accumulated in laser light irradiated sites, suggesting that the ATPase domain of WRNIP1 and ubiquitination of WRNIP1 are dispensable for the accumulation. |
| doi_str_mv | 10.1016/j.bbrc.2011.12.080 |
| format | Article |
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WRNIP1 (Werner helicase-interacting protein 1) was originally identified as a protein that interacts with the Werner syndrome responsible gene product. WRNIP1 contains a ubiquitin-binding zinc-finger (UBZ) domain in the N-terminal region and two leucine zipper motifs in the C-terminal region. In addition, it possesses an ATPase domain in the middle of the molecule and the lysine residues serving as ubiquitin acceptors in the entire of the molecule. Here, we report that WRNIP1 accumulates in laser light irradiated sites very rapidly via its ubiquitin-binding zinc finger domain, which is known to bind polyubiquitin and to be involved in ubiquitination of WRNIP1 itself. The accumulation of WRNIP1 in laser light irradiated sites also required the C-terminal region containing two leucine zippers, which is reportedly involved in the oligomerization of WRNIP1. Mutated WRNIP1 with a deleted ATPase domain or with mutations in lysine residues, which serve as ubiquitin acceptors, accumulated in laser light irradiated sites, suggesting that the ATPase domain of WRNIP1 and ubiquitination of WRNIP1 are dispensable for the accumulation.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/j.bbrc.2011.12.080</identifier><identifier>PMID: 22209848</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>60 APPLIED LIFE SCIENCES ; Adenosine Triphosphatases - genetics ; Adenosine Triphosphatases - metabolism ; ATPase ; ATPases Associated with Diverse Cellular Activities ; Carrier Proteins - genetics ; Carrier Proteins - metabolism ; DNA Damage ; DNA DAMAGES ; DNA-Binding Proteins - genetics ; DNA-Binding Proteins - metabolism ; GENES ; HeLa Cells ; Humans ; IRRADIATION ; LASERS ; LEUCINE ; Leucine Zippers ; Light ; LYSINE ; Lysine - genetics ; Lysine - metabolism ; MOLECULES ; Mutation ; MUTATIONS ; Protein Structure, Tertiary ; PROTEINS ; Ubiquitin ; Ubiquitin - metabolism ; Ubiquitination ; UBZ ; VISIBLE RADIATION ; WRNIP1 ; Zinc Fingers</subject><ispartof>Biochemical and biophysical research communications, 2012-01, Vol.417 (4), p.1145-1150</ispartof><rights>2011 Elsevier Inc.</rights><rights>Copyright © 2011 Elsevier Inc. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c449t-c9cef8d3e6c327401a2d323e9fd2e6fe603624991de62c2f2a7e8bbb38445ce73</citedby><cites>FETCH-LOGICAL-c449t-c9cef8d3e6c327401a2d323e9fd2e6fe603624991de62c2f2a7e8bbb38445ce73</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0006291X11022893$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>230,314,776,780,881,3537,27901,27902,65534</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22209848$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/22207669$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Nomura, Hironoshin</creatorcontrib><creatorcontrib>Yoshimura, Akari</creatorcontrib><creatorcontrib>Edo, Takato</creatorcontrib><creatorcontrib>Kanno, Shin-ichiro</creatorcontrib><creatorcontrib>Tada, Syusuke</creatorcontrib><creatorcontrib>Seki, Masayuki</creatorcontrib><creatorcontrib>Yasui, Akira</creatorcontrib><creatorcontrib>Enomoto, Takemi</creatorcontrib><title>WRNIP1 accumulates at laser light irradiated sites rapidly via its ubiquitin-binding zinc finger domain and independently from its ATPase domain</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>► WRNIP1 accumulates in laser light irradiated sites very rapidly via UBZ domain. ► The ATPase domain of WRNIP1 is dispensable for its accumulation. ► The accumulation of WRNIP1 seems not to be dependent on the interaction with WRN.
WRNIP1 (Werner helicase-interacting protein 1) was originally identified as a protein that interacts with the Werner syndrome responsible gene product. WRNIP1 contains a ubiquitin-binding zinc-finger (UBZ) domain in the N-terminal region and two leucine zipper motifs in the C-terminal region. In addition, it possesses an ATPase domain in the middle of the molecule and the lysine residues serving as ubiquitin acceptors in the entire of the molecule. Here, we report that WRNIP1 accumulates in laser light irradiated sites very rapidly via its ubiquitin-binding zinc finger domain, which is known to bind polyubiquitin and to be involved in ubiquitination of WRNIP1 itself. The accumulation of WRNIP1 in laser light irradiated sites also required the C-terminal region containing two leucine zippers, which is reportedly involved in the oligomerization of WRNIP1. Mutated WRNIP1 with a deleted ATPase domain or with mutations in lysine residues, which serve as ubiquitin acceptors, accumulated in laser light irradiated sites, suggesting that the ATPase domain of WRNIP1 and ubiquitination of WRNIP1 are dispensable for the accumulation.</description><subject>60 APPLIED LIFE SCIENCES</subject><subject>Adenosine Triphosphatases - genetics</subject><subject>Adenosine Triphosphatases - metabolism</subject><subject>ATPase</subject><subject>ATPases Associated with Diverse Cellular Activities</subject><subject>Carrier Proteins - genetics</subject><subject>Carrier Proteins - metabolism</subject><subject>DNA Damage</subject><subject>DNA DAMAGES</subject><subject>DNA-Binding Proteins - genetics</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>GENES</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>IRRADIATION</subject><subject>LASERS</subject><subject>LEUCINE</subject><subject>Leucine Zippers</subject><subject>Light</subject><subject>LYSINE</subject><subject>Lysine - genetics</subject><subject>Lysine - metabolism</subject><subject>MOLECULES</subject><subject>Mutation</subject><subject>MUTATIONS</subject><subject>Protein Structure, Tertiary</subject><subject>PROTEINS</subject><subject>Ubiquitin</subject><subject>Ubiquitin - metabolism</subject><subject>Ubiquitination</subject><subject>UBZ</subject><subject>VISIBLE RADIATION</subject><subject>WRNIP1</subject><subject>Zinc Fingers</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kcFu1DAQhi0EotvCC3BAljhwSrAd48QSl6oqtFIFFSqCm-XYk3ZWibO1nUrlKXhkHHbhyMW2NN__z3h-Ql5xVnPG1btt3ffR1YJxXnNRs449IRvONKsEZ_Ip2TDGVCU0_3FEjlPasgJKpZ-TIyEE053sNuTX96-fL685tc4t0zLaDInaTEebINIRb-8yxRitx1LxNOFaj3aHfnykD2gp5kSXHu8XzBiqHoPHcEt_YnB0KK9i4ufJYqA2eFqqsINyhFzkQ5ynP_rTm-vS7gC-IM8GOyZ4ebhPyLeP5zdnF9XVl0-XZ6dXlZNS58ppB0PnG1CuEa1k3ArfiAb04AWoARRrlJBacw9KODEI20LX933TSfneQduckDd73zllNMmVn7k7N4cALpt1P61SulBv99QuzvcLpGwmTA7G0QaYl2Q073TDu1YWUuxJF-eUIgxmF3Gy8dFwZta4zNascZk1LsOFKXEV0euD_dJP4P9J_uZTgA97AMoqHhDiOikEBx7jOqif8X_-vwG4E6g4</recordid><startdate>20120127</startdate><enddate>20120127</enddate><creator>Nomura, Hironoshin</creator><creator>Yoshimura, Akari</creator><creator>Edo, Takato</creator><creator>Kanno, Shin-ichiro</creator><creator>Tada, Syusuke</creator><creator>Seki, Masayuki</creator><creator>Yasui, Akira</creator><creator>Enomoto, Takemi</creator><general>Elsevier Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>OTOTI</scope></search><sort><creationdate>20120127</creationdate><title>WRNIP1 accumulates at laser light irradiated sites rapidly via its ubiquitin-binding zinc finger domain and independently from its ATPase domain</title><author>Nomura, Hironoshin ; Yoshimura, Akari ; Edo, Takato ; Kanno, Shin-ichiro ; Tada, Syusuke ; Seki, Masayuki ; Yasui, Akira ; Enomoto, Takemi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c449t-c9cef8d3e6c327401a2d323e9fd2e6fe603624991de62c2f2a7e8bbb38445ce73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>60 APPLIED LIFE SCIENCES</topic><topic>Adenosine Triphosphatases - genetics</topic><topic>Adenosine Triphosphatases - metabolism</topic><topic>ATPase</topic><topic>ATPases Associated with Diverse Cellular Activities</topic><topic>Carrier Proteins - genetics</topic><topic>Carrier Proteins - metabolism</topic><topic>DNA Damage</topic><topic>DNA DAMAGES</topic><topic>DNA-Binding Proteins - genetics</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>GENES</topic><topic>HeLa Cells</topic><topic>Humans</topic><topic>IRRADIATION</topic><topic>LASERS</topic><topic>LEUCINE</topic><topic>Leucine Zippers</topic><topic>Light</topic><topic>LYSINE</topic><topic>Lysine - genetics</topic><topic>Lysine - metabolism</topic><topic>MOLECULES</topic><topic>Mutation</topic><topic>MUTATIONS</topic><topic>Protein Structure, Tertiary</topic><topic>PROTEINS</topic><topic>Ubiquitin</topic><topic>Ubiquitin - metabolism</topic><topic>Ubiquitination</topic><topic>UBZ</topic><topic>VISIBLE RADIATION</topic><topic>WRNIP1</topic><topic>Zinc Fingers</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Nomura, Hironoshin</creatorcontrib><creatorcontrib>Yoshimura, Akari</creatorcontrib><creatorcontrib>Edo, Takato</creatorcontrib><creatorcontrib>Kanno, Shin-ichiro</creatorcontrib><creatorcontrib>Tada, Syusuke</creatorcontrib><creatorcontrib>Seki, Masayuki</creatorcontrib><creatorcontrib>Yasui, Akira</creatorcontrib><creatorcontrib>Enomoto, Takemi</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>OSTI.GOV</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Nomura, Hironoshin</au><au>Yoshimura, Akari</au><au>Edo, Takato</au><au>Kanno, Shin-ichiro</au><au>Tada, Syusuke</au><au>Seki, Masayuki</au><au>Yasui, Akira</au><au>Enomoto, Takemi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>WRNIP1 accumulates at laser light irradiated sites rapidly via its ubiquitin-binding zinc finger domain and independently from its ATPase domain</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2012-01-27</date><risdate>2012</risdate><volume>417</volume><issue>4</issue><spage>1145</spage><epage>1150</epage><pages>1145-1150</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>► WRNIP1 accumulates in laser light irradiated sites very rapidly via UBZ domain. ► The ATPase domain of WRNIP1 is dispensable for its accumulation. ► The accumulation of WRNIP1 seems not to be dependent on the interaction with WRN.
WRNIP1 (Werner helicase-interacting protein 1) was originally identified as a protein that interacts with the Werner syndrome responsible gene product. WRNIP1 contains a ubiquitin-binding zinc-finger (UBZ) domain in the N-terminal region and two leucine zipper motifs in the C-terminal region. In addition, it possesses an ATPase domain in the middle of the molecule and the lysine residues serving as ubiquitin acceptors in the entire of the molecule. Here, we report that WRNIP1 accumulates in laser light irradiated sites very rapidly via its ubiquitin-binding zinc finger domain, which is known to bind polyubiquitin and to be involved in ubiquitination of WRNIP1 itself. The accumulation of WRNIP1 in laser light irradiated sites also required the C-terminal region containing two leucine zippers, which is reportedly involved in the oligomerization of WRNIP1. Mutated WRNIP1 with a deleted ATPase domain or with mutations in lysine residues, which serve as ubiquitin acceptors, accumulated in laser light irradiated sites, suggesting that the ATPase domain of WRNIP1 and ubiquitination of WRNIP1 are dispensable for the accumulation.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>22209848</pmid><doi>10.1016/j.bbrc.2011.12.080</doi><tpages>6</tpages></addata></record> |
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| ispartof | Biochemical and biophysical research communications, 2012-01, Vol.417 (4), p.1145-1150 |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | 60 APPLIED LIFE SCIENCES Adenosine Triphosphatases - genetics Adenosine Triphosphatases - metabolism ATPase ATPases Associated with Diverse Cellular Activities Carrier Proteins - genetics Carrier Proteins - metabolism DNA Damage DNA DAMAGES DNA-Binding Proteins - genetics DNA-Binding Proteins - metabolism GENES HeLa Cells Humans IRRADIATION LASERS LEUCINE Leucine Zippers Light LYSINE Lysine - genetics Lysine - metabolism MOLECULES Mutation MUTATIONS Protein Structure, Tertiary PROTEINS Ubiquitin Ubiquitin - metabolism Ubiquitination UBZ VISIBLE RADIATION WRNIP1 Zinc Fingers |
| title | WRNIP1 accumulates at laser light irradiated sites rapidly via its ubiquitin-binding zinc finger domain and independently from its ATPase domain |
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