RRBP1: Difference between revisions

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{{Infobox_gene}}
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'''Ribosome-binding protein 1''', also referred to as '''p180''', is a [[protein]] that in humans is encoded by the ''RRBP1'' [[gene]].<ref name="pmid8812507">{{cite journal |vauthors=Basson CT, MacRae CA, Schoenberg-Fejzo M, Morton CC, Spinner NB, Genin A, Krug E, Seidman JG, Seidman CE | title = Identification, characterization, and chromosomal localization of the human homolog (hES) of ES/130 | journal = Genomics | volume = 35 | issue = 3 | pages = 628–31 |date=Dec 1996 | pmid = 8812507 | pmc =  | doi = 10.1006/geno.1996.0413 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: RRBP1 ribosome binding protein 1 homolog 180kDa (dog)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6238| accessdate = }}</ref>
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{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Ribosome binding protein 1 homolog 180kDa (dog)
| HGNCid = 10448
| Symbol = RRBP1
| AltSymbols =; DKFZp586A1420; ES/130; ES130; FLJ36146; MGC157720; MGC157721; hES
| OMIM = 601418
| ECnumber =
| Homologene = 68138
| MGIid = 1932395
  | GeneAtlas_image1 = PBB_GE_RRBP1_201203_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_RRBP1_201204_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_RRBP1_201206_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005201 |text = extracellular matrix structural constituent}}
| Component = {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005840 |text = ribosome}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0030176 |text = integral to endoplasmic reticulum membrane}}
| Process = {{GNF_GO|id=GO:0006412 |text = translation}} {{GNF_GO|id=GO:0006605 |text = protein targeting}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0015031 |text = protein transport}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 6238
    | Hs_Ensembl = ENSG00000125844
    | Hs_RefseqProtein = NP_001036041
    | Hs_RefseqmRNA = NM_001042576
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 20
    | Hs_GenLoc_start = 17542323
    | Hs_GenLoc_end = 17610878
    | Hs_Uniprot = Q9P2E9
    | Mm_EntrezGene = 81910
    | Mm_Ensembl = ENSMUSG00000027422
    | Mm_RefseqmRNA = XM_622097
    | Mm_RefseqProtein = XP_622097
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 2
    | Mm_GenLoc_start = 143638837
    | Mm_GenLoc_end = 143702690
    | Mm_Uniprot = 
  }}
}}
'''Ribosome binding protein 1 homolog 180kDa (dog)''', also known as '''RRBP1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RRBP1 ribosome binding protein 1 homolog 180kDa (dog)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6238| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = Analysis of cDNA clones indicates that ribosome binding protein 1 may exist in different forms due to removal of tandem repeats, or partial intraexonic splicing of RRBP1. The form presented here is lacking the canine p180 ribosome-binding domain, NQGKKAEGAQ, which is tandemly repeated close to the N-terminus in other forms that haven't been fully characterized. RRBP1 has been excluded as a candidate gene in the cause of Alagille syndrome. Alternate splicing results in multiple transcript variants.<ref name="entrez">{{cite web | title = Entrez Gene: RRBP1 ribosome binding protein 1 homolog 180kDa (dog)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6238| accessdate = }}</ref>
| summary_text = RRBP1 is a membrane-bound protein found in the [[endoplasmic reticulum]] (ER). It was originally identified as the ribosome receptor for the ER,<ref name="SavitzMeyer1990">{{cite journal|last1=Savitz|first1=Adam J.|last2=Meyer|first2=David I.|title=Identification of a ribosome receptor in the rough endoplasmic reticulum|journal=Nature|volume=346|issue=6284|year=1990|pages=540–544|issn=0028-0836|doi=10.1038/346540a0|pmid=2165568}}</ref> however several groups later demonstrated that this activity did not co-fractionate with RRBP1 <ref name="NunnariZimmerman1991">{{cite journal|last1=Nunnari|first1=Jodi M.|last2=Zimmerman|first2=Deborah L.|last3=Ogg|first3=Stephen C.|last4=Walter|first4=Peter|title=Characterization of the rough endoplasmic reticulum ribosome-binding activity|journal=Nature|volume=352|issue=6336|year=1991|pages=638–640|issn=0028-0836|doi=10.1038/352638a0|pmid=1650916}}</ref>
}}
<ref name="CollinsGilmore1991">{{cite journal|last1=Collins|first1=PG|last2=Gilmore|first2=R L|title=Ribosome binding to the endoplasmic reticulum: a 180-kD protein identified by crosslinking to membrane-bound ribosomes is not required for ribosome binding activity|journal=JCB|volume=114|issue=4|year=1991|pages=639–49|issn=|doi=10.1083/jcb.114.4.639}}</ref> but rather with [[Sec61]] (i.e. the [[translocon]]).<ref name="GörlichPrehn1992">{{cite journal|last1=Görlich|first1=Dirk|last2=Prehn|first2=Siegfried|last3=Hartmann|first3=Enno|last4=Kalies|first4=Kai-Uwe|last5=Rapoport|first5=Tom A.|title=A mammalian homolog of SEC61p and SECYp is associated with ribosomes and nascent polypeptides during translocation|journal=Cell|volume=71|issue=3|year=1992|pages=489–503|issn=0092-8674|doi=10.1016/0092-8674(92)90517-G|pmid=1423609}}</ref><ref name="Gorlich1993">{{cite journal|last1=Gorlich|first1=D|title=Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane|journal=Cell|volume=75|issue=4|year=1993|pages=615–630|issn=0092-8674|doi=10.1016/0092-8674(93)90483-7|pmid=8242738}}</ref> RRBP1 can enhance the association of certain mRNAs to the endoplasmic reticulum in a manner that does not require ribosome activity, likely by directly associating the mRNA's phosphate backbone<ref name="Cui2012">{{cite journal|last1=Cui|first1=Xianying A.|last2=Zhang|first2=Hui|last3=Palazzo|first3=Alexander F.|title=p180 Promotes the Ribosome-Independent Localization of a Subset of mRNA to the Endoplasmic Reticulum|journal=PLoS Biology|volume=10|issue=5|year=2012|pages=e1001336|issn=1545-7885|doi=10.1371/journal.pbio.1001336|pmid=22679391|pmc=3362647}}</ref>}}. In addition, RRBP1 may promote the association of polysomes with the translocon <ref name="DejgaardTheberge2010">{{cite journal|last1=Dejgaard|first1=Kurt|last2=Theberge|first2=Jean-Francois|last3=Heath-Engel|first3=Hannah|last4=Chevet|first4=Eric|last5=Tremblay|first5=Michel L.|last6=Thomas|first6=David Y.|title=Organization of the Sec61 Translocon, Studied by High Resolution Native Electrophoresis|journal=Journal of Proteome Research|volume=9|issue=4|year=2010|pages=1763–1771|issn=1535-3893|doi=10.1021/pr900900x|pmid=20112977}}</ref><ref name="UenoKaneko2011">{{cite journal|last1=Ueno|first1=T.|last2=Kaneko|first2=K.|last3=Sata|first3=T.|last4=Hattori|first4=S.|last5=Ogawa-Goto|first5=K.|title=Regulation of polysome assembly on the endoplasmic reticulum by a coiled-coil protein, p180|journal=Nucleic Acids Research|volume=40|issue=7|year=2011|pages=3006–3017|issn=0305-1048|doi=10.1093/nar/gkr1197|pmid=22156060|pmc=3326322}}</ref> and play a role in ER morphology.<ref name="ShibataShemesh2010">{{cite journal|last1=Shibata|first1=Yoko|last2=Shemesh|first2=Tom|last3=Prinz|first3=William A.|last4=Palazzo|first4=Alexander F.|last5=Kozlov|first5=Michael M.|last6=Rapoport|first6=Tom A.|title=Mechanisms Determining the Morphology of the Peripheral ER|journal=Cell|volume=143|issue=5|year=2010|pages=774–788|issn=0092-8674|doi=10.1016/j.cell.2010.11.007}}</ref> RRBP1 may also bind to [[microtubules]].<ref name="Ogawa-GotoUeno2007">{{cite journal  |vauthors=Ogawa-Goto K, Tanaka K, Ueno T, etal |title=p180 Is Involved in the Interaction between the Endoplasmic Reticulum and Microtubules through a Novel Microtubule-binding and Bundling Domain |journal=Mol. Biol. Cell |volume=18 |issue= 10 |pages= 3741–51 |year= 2007 |pmid= 17634287 |doi= 10.1091/mbc.E06-12-1125  | pmc=1995732 }}</ref> Although the p180 isoform is the most abundant, it may exist in different forms due to removal of tandem repeats by partial intraexonic splicing. RRBP1 has been excluded as a candidate gene in the cause of Alagille syndrome.<ref name="entrez" />


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
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| citations =  
| citations =  
*{{cite journal | author=Nakajima D, Okazaki N, Yamakawa H, ''et al.'' |title=Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. |journal=DNA Res. |volume=9 |issue= 3 |pages= 99-106 |year= 2003 |pmid= 12168954 |doi=  }}
*{{cite journal   |vauthors=Nakajima D, Okazaki N, Yamakawa H, etal |title=Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones |journal=DNA Res. |volume=9 |issue= 3 |pages= 99–106 |year= 2003 |pmid= 12168954 |doi=10.1093/dnares/9.3.99 }}
*{{cite journal  | author=Savitz AJ, Meyer DI |title=Identification of a ribosome receptor in the rough endoplasmic reticulum. |journal=Nature |volume=346 |issue= 6284 |pages= 540-4 |year= 1990 |pmid= 2165568 |doi= 10.1038/346540a0 }}
*{{cite journal  |vauthors=Savitz AJ, Meyer DI |title=Identification of a ribosome receptor in the rough endoplasmic reticulum |journal=Nature |volume=346 |issue= 6284 |pages= 540–4 |year= 1990 |pmid= 2165568 |doi= 10.1038/346540a0 }}
*{{cite journal | author=Basson CT, MacRae CA, Schoenberg-Fejzo M, ''et al.'' |title=Identification, characterization, and chromosomal localization of the human homolog (hES) of ES/130. |journal=Genomics |volume=35 |issue= 3 |pages= 628-31 |year= 1996 |pmid= 8812507 |doi= 10.1006/geno.1996.0413 }}
*{{cite journal   |vauthors=Langley R, Leung E, Morris C, etal |title=Identification of multiple forms of 180-kDa ribosome receptor in human cells |journal=DNA Cell Biol. |volume=17 |issue= 5 |pages= 449–60 |year= 1998 |pmid= 9628588 |doi=10.1089/dna.1998.17.449 }}
*{{cite journal  | author=Langley R, Leung E, Morris C, ''et al.'' |title=Identification of multiple forms of 180-kDa ribosome receptor in human cells. |journal=DNA Cell Biol. |volume=17 |issue= 5 |pages= 449-60 |year= 1998 |pmid= 9628588 |doi=  }}
*{{cite journal   |vauthors=Nagase T, Kikuno R, Ishikawa KI, etal |title=Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro |journal=DNA Res. |volume=7 |issue= 1 |pages= 65–73 |year= 2000 |pmid= 10718198 |doi=10.1093/dnares/7.1.65 }}
*{{cite journal | author=Nagase T, Kikuno R, Ishikawa KI, ''et al.'' |title=Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro. |journal=DNA Res. |volume=7 |issue= 1 |pages= 65-73 |year= 2000 |pmid= 10718198 |doi=  }}
*{{cite journal   |vauthors=Deloukas P, Matthews LH, Ashurst J, etal |title=The DNA sequence and comparative analysis of human chromosome 20 |journal=Nature |volume=414 |issue= 6866 |pages= 865–71 |year= 2002 |pmid= 11780052 |doi= 10.1038/414865a }}
*{{cite journal | author=Deloukas P, Matthews LH, Ashurst J, ''et al.'' |title=The DNA sequence and comparative analysis of human chromosome 20. |journal=Nature |volume=414 |issue= 6866 |pages= 865-71 |year= 2002 |pmid= 11780052 |doi= 10.1038/414865a }}
*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal   |vauthors=Ota T, Suzuki Y, Nishikawa T, etal |title=Complete sequencing and characterization of 21,243 full-length human cDNAs |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  |vauthors=Diefenbach RJ, Diefenbach E, Douglas MW, Cunningham AL |title=The ribosome receptor, p180, interacts with kinesin heavy chain, KIF5B |journal=Biochem. Biophys. Res. Commun. |volume=319 |issue= 3 |pages= 987–92 |year= 2004 |pmid= 15184079 |doi= 10.1016/j.bbrc.2004.05.069 }}
*{{cite journal  | author=Diefenbach RJ, Diefenbach E, Douglas MW, Cunningham AL |title=The ribosome receptor, p180, interacts with kinesin heavy chain, KIF5B. |journal=Biochem. Biophys. Res. Commun. |volume=319 |issue= 3 |pages= 987-92 |year= 2004 |pmid= 15184079 |doi= 10.1016/j.bbrc.2004.05.069 }}
*{{cite journal   |vauthors=Colland F, Jacq X, Trouplin V, etal |title=Functional Proteomics Mapping of a Human Signaling Pathway |journal=Genome Res. |volume=14 |issue= 7 |pages= 1324–32 |year= 2004 |pmid= 15231748 |doi= 10.1101/gr.2334104 | pmc=442148 }}
*{{cite journal | author=Colland F, Jacq X, Trouplin V, ''et al.'' |title=Functional proteomics mapping of a human signaling pathway. |journal=Genome Res. |volume=14 |issue= 7 |pages= 1324-32 |year= 2004 |pmid= 15231748 |doi= 10.1101/gr.2334104 }}
*{{cite journal   |vauthors=Beausoleil SA, Jedrychowski M, Schwartz D, etal |title=Large-scale characterization of HeLa cell nuclear phosphoproteins |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 33 |pages= 12130–5 |year= 2004 |pmid= 15302935 |doi= 10.1073/pnas.0404720101 | pmc=514446 }}
*{{cite journal | author=Beausoleil SA, Jedrychowski M, Schwartz D, ''et al.'' |title=Large-scale characterization of HeLa cell nuclear phosphoproteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 33 |pages= 12130-5 |year= 2004 |pmid= 15302935 |doi= 10.1073/pnas.0404720101 }}
*{{cite journal   |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal   |vauthors=Beausoleil SA, Villén J, Gerber SA, etal |title=A probability-based approach for high-throughput protein phosphorylation analysis and site localization |journal=Nat. Biotechnol. |volume=24 |issue= 10 |pages= 1285–92 |year= 2006 |pmid= 16964243 |doi= 10.1038/nbt1240 }}
*{{cite journal | author=Beausoleil SA, Villén J, Gerber SA, ''et al.'' |title=A probability-based approach for high-throughput protein phosphorylation analysis and site localization. |journal=Nat. Biotechnol. |volume=24 |issue= 10 |pages= 1285-92 |year= 2006 |pmid= 16964243 |doi= 10.1038/nbt1240 }}
*{{cite journal   |vauthors=Olsen JV, Blagoev B, Gnad F, etal |title=Global, in vivo, and site-specific phosphorylation dynamics in signaling networks |journal=Cell |volume=127 |issue= 3 |pages= 635–48 |year= 2006 |pmid= 17081983 |doi= 10.1016/j.cell.2006.09.026 }}
*{{cite journal | author=Olsen JV, Blagoev B, Gnad F, ''et al.'' |title=Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. |journal=Cell |volume=127 |issue= 3 |pages= 635-48 |year= 2006 |pmid= 17081983 |doi= 10.1016/j.cell.2006.09.026 }}
*{{cite journal   |vauthors=Ewing RM, Chu P, Elisma F, etal |title=Large-scale mapping of human protein–protein interactions by mass spectrometry |journal=Mol. Syst. Biol. |volume=3 |issue=  1|pages= 89 |year= 2007 |pmid= 17353931 |doi= 10.1038/msb4100134  | pmc=1847948 }}
*{{cite journal | author=Ewing RM, Chu P, Elisma F, ''et al.'' |title=Large-scale mapping of human protein-protein interactions by mass spectrometry. |journal=Mol. Syst. Biol. |volume=3 |issue=  |pages= 89 |year= 2007 |pmid= 17353931 |doi= 10.1038/msb4100134 }}
*{{cite journal | author=Ogawa-Goto K, Tanaka K, Ueno T, ''et al.'' |title=p180 is involved in the interaction between the endoplasmic reticulum and microtubules through a novel microtubule-binding and bundling domain. |journal=Mol. Biol. Cell |volume=18 |issue= 10 |pages= 3741-51 |year= 2007 |pmid= 17634287 |doi= 10.1091/mbc.E06-12-1125 }}
}}
}}
{{refend}}
{{refend}}


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Revision as of 09:29, 10 September 2017

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External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
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View/Edit Human

Ribosome-binding protein 1, also referred to as p180, is a protein that in humans is encoded by the RRBP1 gene.[1][2]

RRBP1 is a membrane-bound protein found in the endoplasmic reticulum (ER). It was originally identified as the ribosome receptor for the ER,[3] however several groups later demonstrated that this activity did not co-fractionate with RRBP1 [4] [5] but rather with Sec61 (i.e. the translocon).[6][7] RRBP1 can enhance the association of certain mRNAs to the endoplasmic reticulum in a manner that does not require ribosome activity, likely by directly associating the mRNA's phosphate backbone[8]. In addition, RRBP1 may promote the association of polysomes with the translocon [9][10] and play a role in ER morphology.[11] RRBP1 may also bind to microtubules.[12] Although the p180 isoform is the most abundant, it may exist in different forms due to removal of tandem repeats by partial intraexonic splicing. RRBP1 has been excluded as a candidate gene in the cause of Alagille syndrome.[2]

References

  1. ↑ Basson CT, MacRae CA, Schoenberg-Fejzo M, Morton CC, Spinner NB, Genin A, Krug E, Seidman JG, Seidman CE (Dec 1996). "Identification, characterization, and chromosomal localization of the human homolog (hES) of ES/130". Genomics. 35 (3): 628–31. doi:10.1006/geno.1996.0413. PMID 8812507.
  2. ↑ 2.0 2.1 "Entrez Gene: RRBP1 ribosome binding protein 1 homolog 180kDa (dog)".
  3. ↑ Savitz, Adam J.; Meyer, David I. (1990). "Identification of a ribosome receptor in the rough endoplasmic reticulum". Nature. 346 (6284): 540–544. doi:10.1038/346540a0. ISSN 0028-0836. PMID 2165568.
  4. ↑ Nunnari, Jodi M.; Zimmerman, Deborah L.; Ogg, Stephen C.; Walter, Peter (1991). "Characterization of the rough endoplasmic reticulum ribosome-binding activity". Nature. 352 (6336): 638–640. doi:10.1038/352638a0. ISSN 0028-0836. PMID 1650916.
  5. ↑ Collins, PG; Gilmore, R L (1991). "Ribosome binding to the endoplasmic reticulum: a 180-kD protein identified by crosslinking to membrane-bound ribosomes is not required for ribosome binding activity". JCB. 114 (4): 639–49. doi:10.1083/jcb.114.4.639.
  6. ↑ Görlich, Dirk; Prehn, Siegfried; Hartmann, Enno; Kalies, Kai-Uwe; Rapoport, Tom A. (1992). "A mammalian homolog of SEC61p and SECYp is associated with ribosomes and nascent polypeptides during translocation". Cell. 71 (3): 489–503. doi:10.1016/0092-8674(92)90517-G. ISSN 0092-8674. PMID 1423609.
  7. ↑ Gorlich, D (1993). "Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane". Cell. 75 (4): 615–630. doi:10.1016/0092-8674(93)90483-7. ISSN 0092-8674. PMID 8242738.
  8. ↑ Cui, Xianying A.; Zhang, Hui; Palazzo, Alexander F. (2012). "p180 Promotes the Ribosome-Independent Localization of a Subset of mRNA to the Endoplasmic Reticulum". PLoS Biology. 10 (5): e1001336. doi:10.1371/journal.pbio.1001336. ISSN 1545-7885. PMC 3362647. PMID 22679391.
  9. ↑ Dejgaard, Kurt; Theberge, Jean-Francois; Heath-Engel, Hannah; Chevet, Eric; Tremblay, Michel L.; Thomas, David Y. (2010). "Organization of the Sec61 Translocon, Studied by High Resolution Native Electrophoresis". Journal of Proteome Research. 9 (4): 1763–1771. doi:10.1021/pr900900x. ISSN 1535-3893. PMID 20112977.
  10. ↑ Ueno, T.; Kaneko, K.; Sata, T.; Hattori, S.; Ogawa-Goto, K. (2011). "Regulation of polysome assembly on the endoplasmic reticulum by a coiled-coil protein, p180". Nucleic Acids Research. 40 (7): 3006–3017. doi:10.1093/nar/gkr1197. ISSN 0305-1048. PMC 3326322. PMID 22156060.
  11. ↑ Shibata, Yoko; Shemesh, Tom; Prinz, William A.; Palazzo, Alexander F.; Kozlov, Michael M.; Rapoport, Tom A. (2010). "Mechanisms Determining the Morphology of the Peripheral ER". Cell. 143 (5): 774–788. doi:10.1016/j.cell.2010.11.007. ISSN 0092-8674.
  12. ↑ Ogawa-Goto K, Tanaka K, Ueno T, et al. (2007). "p180 Is Involved in the Interaction between the Endoplasmic Reticulum and Microtubules through a Novel Microtubule-binding and Bundling Domain". Mol. Biol. Cell. 18 (10): 3741–51. doi:10.1091/mbc.E06-12-1125. PMC 1995732. PMID 17634287.

Further reading


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