publication . Article . Other literature type . 2017

Cell Signalling Pathway Regulation by RanBPM: Molecular Insights and Disease Implications

Salemi, Louisa M.; Maitland, Matthew E. R.; McTavish, Christina J.; Schild-Poulter, Caroline;
Open Access
  • Published: 28 Jun 2017 Journal: Open Biology, volume 7, page 170,081 (issn: 2046-2441, eissn: 2046-2441, Copyright policy)
  • Publisher: The Royal Society
Abstract
RanBPM (Ran-binding protein M, also called RanBP9) is an evolutionarily conserved, ubiquitous protein which localizes to both nucleus and cytoplasm. RanBPM has been implicated in the regulation of a number of signalling pathways to regulate several cellular processes such as apoptosis, cell adhesion, migration as well as transcription, and plays a critical role during development. In addition, RanBPM has been shown to regulate pathways implicated in cancer and Alzheimer's disease, implying that RanBPM has important functions in both normal and pathological development. While its functions in these processes are still poorly understood, RanBPM has been identified...
Subjects
free text keywords: Disease, Cell biology, Signal transducing adaptor protein, Protein M, Nucleus, medicine.anatomical_structure, medicine, Mutation, medicine.disease_cause, Molecular biology, Biology, Conserved sequence, Cell signaling, Cytoplasm, 33, 15, 129, Review, Review Article, RanBPM, CTLH complex, Gid, cancer, Alzheimer disease
Related Organizations
Funded by
CIHR
Project
  • Funder: Canadian Institutes of Health Research (CIHR)
143 references, page 1 of 10

1 Nakamura M et al.1998 When overexpressed, a novel centrosomal protein, RanBPM, causes ectopi c microtubule nucleation similar to gamma-tubulin. J. Cell Biol.143, 1041–1052. (doi:10.1083/jcb.143.4.1041)9817760 [OpenAIRE] [PubMed]

2 Nishitani H, Hirose E, Uchimura Y, Nakamura M, Umeda M, Nishii K, Mori N, Nishimoto T 2001 Full-sized RanBPM cDNA encodes a protein possessing a long stretch of proline and glutamine within the N-terminal region, comprising a large protein complex. Gene 272, 25–33. (doi:10.1016/S0378-1119(01)00553-4)11470507 [OpenAIRE] [PubMed]

3 Santt O, Pfirrmann T, Braun B, Juretschke J, Kimmig P, Scheel H, Hofmann K, Thumm M, Wolf DH 2008 The yeast GID complex, a novel ubiquitin ligase (E3) involved in the regulation of carbohydrate metabolism. Mol. Biol. Cell 19, 3323–3333. (doi:10.1091/mbc.E08-03-0328)18508925 [OpenAIRE] [PubMed]

4 Salemi LM, Loureiro SO, Schild-Poulter C 2015 Characterization of RanBPM molecular determinants that control its subcellular localization. PLoS ONE 10, e0117655 (doi:10.1371/journal.pone.0117655)25659156 [OpenAIRE] [PubMed]

5 Atabakhsh E, Bryce DM, Lefebvre KJ, Schild-Poulter C 2009 RanBPM has proapoptotic activities that regulate cell death pathways in response to DNA damage. Mol. Cancer Res.7, 1962–1972. (doi:10.1158/1541-7786.MCR-09-0098)19996306 [OpenAIRE] [PubMed]

6 Kallberg M, Wang H, Wang S, Peng J, Wang Z, Lu H, Xu J 2012 Template-based protein structure modeling using the RaptorX web server. Nat. Protoc.7, 1511–1522. (doi:10.1038/nprot.2012.085)22814390 [OpenAIRE] [PubMed]

7 Ma J, Wang S, Zhao F, Xu J 2013 Protein threading using context-specific alignment potential. Bioinformatics 29, i257–i265. (doi:10.1093/bioinformatics/btt210)23812991 [OpenAIRE] [PubMed]

8 Peng J, Xu J 2011 A multiple-template approach to protein threading. Proteins 79, 1930–1939. (doi:10.1002/prot.23016)21465564 [OpenAIRE] [PubMed]

9 Peng J, Xu J 20 11 Raptorx: Exploiting structure information for protein alignment by statistical inference. Proteins 79(Suppl. 10), 161–171. (doi:10.1002/prot.23175)21987485 [OpenAIRE] [PubMed]

10 Kay BK, Williamson MP, Sudol M 2000 The importance of being proline: the interaction of proline-rich motifs in signaling proteins with their cognate domains. FASEB J.14, 231–241. (doi:10.1096/fj.1530-6860)10657980 [OpenAIRE] [PubMed]

11 Murrin LC, Talbot JN 2007 RanBPM, a scaffolding protein in the immune and nervous systems. J. Neuroimmune Pharmacol.2, 290–295. (doi:10.1007/s11481-007-9079-x)1804 0864 [OpenAIRE] [PubMed]

12 Hilton DJ et al.1998 Twenty proteins containing a C-terminal SOCS box form five structural classes. Proc. Natl Acad. Sci. USA 95, 114–119. (doi:10.1073/pnas.95.1.114)9419338 [OpenAIRE] [PubMed]

13 Menon RP, Gibson TJ, Pastore A 2004 The C terminus of fragile X mental retardation protein interacts with the multi-domain Ran-binding protein in the microtubule-organising centre. J. Mol. Biol.343, 43–53. (doi:10.1016/j.jmb.2004.08.024)15381419 [OpenAIRE] [PubMed]

14 Perfetto L, Gherardini PF, Davey NE, Diella F, Helmer-Citterich M, Cesareni G 2013 Exploring the diversity of SPRY/B30.2-mediated interactions. Trends Biochem. Sci.38, 38–46. (doi:10.1016/j.tibs.2012.10.001)23164942 [OpenAIRE] [PubMed]

15 Ponting C, Schultz J, Bork P 1997 SPRY domains in ryanodine receptors (Ca 2+-release channels). Trends Biochem. Sci.22, 193–194. (doi:10.1016/s0968-0004(97)01049-9)9204703 [OpenAIRE] [PubMed]

143 references, page 1 of 10
Abstract
RanBPM (Ran-binding protein M, also called RanBP9) is an evolutionarily conserved, ubiquitous protein which localizes to both nucleus and cytoplasm. RanBPM has been implicated in the regulation of a number of signalling pathways to regulate several cellular processes such as apoptosis, cell adhesion, migration as well as transcription, and plays a critical role during development. In addition, RanBPM has been shown to regulate pathways implicated in cancer and Alzheimer's disease, implying that RanBPM has important functions in both normal and pathological development. While its functions in these processes are still poorly understood, RanBPM has been identified...
Subjects
free text keywords: Disease, Cell biology, Signal transducing adaptor protein, Protein M, Nucleus, medicine.anatomical_structure, medicine, Mutation, medicine.disease_cause, Molecular biology, Biology, Conserved sequence, Cell signaling, Cytoplasm, 33, 15, 129, Review, Review Article, RanBPM, CTLH complex, Gid, cancer, Alzheimer disease
Related Organizations
Funded by
CIHR
Project
  • Funder: Canadian Institutes of Health Research (CIHR)
143 references, page 1 of 10

1 Nakamura M et al.1998 When overexpressed, a novel centrosomal protein, RanBPM, causes ectopi c microtubule nucleation similar to gamma-tubulin. J. Cell Biol.143, 1041–1052. (doi:10.1083/jcb.143.4.1041)9817760 [OpenAIRE] [PubMed]

2 Nishitani H, Hirose E, Uchimura Y, Nakamura M, Umeda M, Nishii K, Mori N, Nishimoto T 2001 Full-sized RanBPM cDNA encodes a protein possessing a long stretch of proline and glutamine within the N-terminal region, comprising a large protein complex. Gene 272, 25–33. (doi:10.1016/S0378-1119(01)00553-4)11470507 [OpenAIRE] [PubMed]

3 Santt O, Pfirrmann T, Braun B, Juretschke J, Kimmig P, Scheel H, Hofmann K, Thumm M, Wolf DH 2008 The yeast GID complex, a novel ubiquitin ligase (E3) involved in the regulation of carbohydrate metabolism. Mol. Biol. Cell 19, 3323–3333. (doi:10.1091/mbc.E08-03-0328)18508925 [OpenAIRE] [PubMed]

4 Salemi LM, Loureiro SO, Schild-Poulter C 2015 Characterization of RanBPM molecular determinants that control its subcellular localization. PLoS ONE 10, e0117655 (doi:10.1371/journal.pone.0117655)25659156 [OpenAIRE] [PubMed]

5 Atabakhsh E, Bryce DM, Lefebvre KJ, Schild-Poulter C 2009 RanBPM has proapoptotic activities that regulate cell death pathways in response to DNA damage. Mol. Cancer Res.7, 1962–1972. (doi:10.1158/1541-7786.MCR-09-0098)19996306 [OpenAIRE] [PubMed]

6 Kallberg M, Wang H, Wang S, Peng J, Wang Z, Lu H, Xu J 2012 Template-based protein structure modeling using the RaptorX web server. Nat. Protoc.7, 1511–1522. (doi:10.1038/nprot.2012.085)22814390 [OpenAIRE] [PubMed]

7 Ma J, Wang S, Zhao F, Xu J 2013 Protein threading using context-specific alignment potential. Bioinformatics 29, i257–i265. (doi:10.1093/bioinformatics/btt210)23812991 [OpenAIRE] [PubMed]

8 Peng J, Xu J 2011 A multiple-template approach to protein threading. Proteins 79, 1930–1939. (doi:10.1002/prot.23016)21465564 [OpenAIRE] [PubMed]

9 Peng J, Xu J 20 11 Raptorx: Exploiting structure information for protein alignment by statistical inference. Proteins 79(Suppl. 10), 161–171. (doi:10.1002/prot.23175)21987485 [OpenAIRE] [PubMed]

10 Kay BK, Williamson MP, Sudol M 2000 The importance of being proline: the interaction of proline-rich motifs in signaling proteins with their cognate domains. FASEB J.14, 231–241. (doi:10.1096/fj.1530-6860)10657980 [OpenAIRE] [PubMed]

11 Murrin LC, Talbot JN 2007 RanBPM, a scaffolding protein in the immune and nervous systems. J. Neuroimmune Pharmacol.2, 290–295. (doi:10.1007/s11481-007-9079-x)1804 0864 [OpenAIRE] [PubMed]

12 Hilton DJ et al.1998 Twenty proteins containing a C-terminal SOCS box form five structural classes. Proc. Natl Acad. Sci. USA 95, 114–119. (doi:10.1073/pnas.95.1.114)9419338 [OpenAIRE] [PubMed]

13 Menon RP, Gibson TJ, Pastore A 2004 The C terminus of fragile X mental retardation protein interacts with the multi-domain Ran-binding protein in the microtubule-organising centre. J. Mol. Biol.343, 43–53. (doi:10.1016/j.jmb.2004.08.024)15381419 [OpenAIRE] [PubMed]

14 Perfetto L, Gherardini PF, Davey NE, Diella F, Helmer-Citterich M, Cesareni G 2013 Exploring the diversity of SPRY/B30.2-mediated interactions. Trends Biochem. Sci.38, 38–46. (doi:10.1016/j.tibs.2012.10.001)23164942 [OpenAIRE] [PubMed]

15 Ponting C, Schultz J, Bork P 1997 SPRY domains in ryanodine receptors (Ca 2+-release channels). Trends Biochem. Sci.22, 193–194. (doi:10.1016/s0968-0004(97)01049-9)9204703 [OpenAIRE] [PubMed]

143 references, page 1 of 10
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publication . Article . Other literature type . 2017

Cell Signalling Pathway Regulation by RanBPM: Molecular Insights and Disease Implications

Salemi, Louisa M.; Maitland, Matthew E. R.; McTavish, Christina J.; Schild-Poulter, Caroline;