WIPI2: Difference between revisions

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{{Infobox_gene}}
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'''WD repeat domain phosphoinositide-interacting protein 2''' is a [[protein]] that in humans is encoded by the ''WIPI2'' [[gene]].<ref name="pmid15602573">{{cite journal |vauthors=Proikas-Cezanne T, Waddell S, Gaugel A, Frickey T, Lupas A, Nordheim A | title = WIPI-1alpha (WIPI49), a member of the novel 7-bladed WIPI protein family, is aberrantly expressed in human cancer and is linked to starvation-induced autophagy | journal = Oncogene | volume = 23 | issue = 58 | pages = 9314–25 |date=Dec 2004 | pmid = 15602573 | pmc =  | doi = 10.1038/sj.onc.1208331 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: WIPI2 WD repeat domain, phosphoinositide interacting 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=26100| accessdate = }}</ref>
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== Function ==
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[[WD40 repeat]] proteins are key components of many essential biologic functions. They regulate the assembly of multiprotein complexes by presenting a beta-propeller platform for simultaneous and reversible protein-protein interactions. Members of the WIPI subfamily of WD40 repeat proteins, such as WIPI2, have a 7-bladed propeller structure and contain a conserved motif for interaction with phospholipids.<ref name="pmid15602573"/><ref name="entrez"/>
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WIPI2 is the mammalian homolog of Atg18, not Atg21, along with the closely related protein, [[WIPI1]]. WIPI2 mRNA is readily detectable in several commonly used laboratory cell lines (HEK293A, HeLa, A431) and several cancer cell lines, while WIPI1 expression is limited to cancer cells.


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The Atg proteins regulate [[autophagy]], which is a [[lysosome|lysosomal]] degradation pathway required for maintaining cell health, surviving periods of nutrient deprivation and also plays a role in cancer, neurodegeneration and immune responses to a diverse range of pathogens.<ref name="pmid20036114">{{cite journal |vauthors=Orsi A, Polson HE, Tooze SA | title = Membrane trafficking events that partake in autophagy | journal = Curr Opin Cell Biol | volume = 22| issue = 2| pages = 150–6|date=December 2009 | pmid = 20036114 | doi = 10.1016/j.ceb.2009.11.013 | url =  }}</ref> WIPI2 is recruited early to the forming autophagosome, along with DFCP-1, ULK-1 and Atg16, where it positively regulates the lipidation of Atg8 (LC3). This is not true for WIPI1.
{{GNF_Protein_box
| image =
| image_source = 
| PDB =  
| Name = WD repeat domain, phosphoinositide interacting 2
| HGNCid = 32225
| Symbol = WIPI2
| AltSymbols =; Atg21; CGI-50; DKFZP434J154; DKFZp686P02188; FLJ12979; FLJ14217; FLJ42984; WIPI-2
| OMIM = 609225
| ECnumber =
| Homologene = 69189
| MGIid = 1923831
| GeneAtlas_image1 = PBB_GE_WIPI2_202031_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_WIPI2_204710_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_WIPI2_214699_x_at_tn.png
| Function =
| Component = {{GNF_GO|id=GO:0043234 |text = protein complex}}
| Process =
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 26100
    | Hs_Ensembl = ENSG00000157954
    | Hs_RefseqProtein = NP_001028690
    | Hs_RefseqmRNA = NM_001033518
    | Hs_GenLoc_db =   
    | Hs_GenLoc_chr = 7
    | Hs_GenLoc_start = 5196361
    | Hs_GenLoc_end = 5240012
    | Hs_Uniprot = Q9Y4P8
    | Mm_EntrezGene = 74781
    | Mm_Ensembl = ENSMUSG00000029578
    | Mm_RefseqmRNA = NM_178398
    | Mm_RefseqProtein = NP_848485
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 5
    | Mm_GenLoc_start = 142882057
    | Mm_GenLoc_end = 142921857
    | Mm_Uniprot = Q80W47
  }}
}}
'''WD repeat domain, phosphoinositide interacting 2''', also known as '''WIPI2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: WIPI2 WD repeat domain, phosphoinositide interacting 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=26100| accessdate = }}</ref>


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== See also ==
{{PBB_Summary
* [[WIPI protein family]]
| section_title =  
| summary_text = WD40 repeat proteins are key components of many essential biologic functions. They regulate the assembly of multiprotein complexes by presenting a beta-propeller platform for simultaneous and reversible protein-protein interactions. Members of the WIPI subfamily of WD40 repeat proteins, such as WIPI2, have a 7-bladed propeller structure and contain a conserved motif for interaction with phospholipids (Proikas-Cezanne et al., 2004).[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: WIPI2 WD repeat domain, phosphoinositide interacting 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=26100| accessdate = }}</ref>
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
* {{cite journal | pmid = 20505359 | doi=10.4161/auto.6.4.11863 | volume=6 | title=Mammalian Atg18 (WIPI2) localizes to omegasome-anchored phagophores and positively regulates LC3 lipidation | year=2010 | journal=Autophagy | pages=506–22 |vauthors=Polson HE, de Lartigue J, Rigden DJ, Reedijk M, Urbé S, Clague MJ, Tooze SA }}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Mehrle A, Rosenfelder H, Schupp I, ''et al.'' |title=The LIFEdb database in 2006. |journal=Nucleic Acids Res. |volume=34 |issue= Database issue |pages= D415-8 |year= 2006 |pmid= 16381901 |doi= 10.1093/nar/gkj139 }}
*{{cite journal  | author=Mehrle A |title=The LIFEdb database in 2006 |journal=Nucleic Acids Res. |volume=34 |issue= Database issue |pages= D415–8 |year= 2006 |pmid= 16381901 |doi= 10.1093/nar/gkj139  | pmc=1347501  |name-list-format=vanc| author2=Rosenfelder H  | author3=Schupp I  | display-authors=3  | last4=Del Val  | first4=C  | last5=Arlt  | first5=D  | last6=Hahne  | first6=F  | last7=Bechtel  | first7=S  | last8=Simpson  | first8=J  | last9=Hofmann  | first9=O }}
*{{cite journal | author=Proikas-Cezanne T, Waddell S, Gaugel A, ''et al.'' |title=WIPI-1alpha (WIPI49), a member of the novel 7-bladed WIPI protein family, is aberrantly expressed in human cancer and is linked to starvation-induced autophagy. |journal=Oncogene |volume=23 |issue= 58 |pages= 9314-25 |year= 2005 |pmid= 15602573 |doi= 10.1038/sj.onc.1208331 }}
*{{cite journal  | author=Wiemann S |title=From ORFeome to Biology: A Functional Genomics Pipeline |journal=Genome Res. |volume=14 |issue= 10B |pages= 2136–44 |year= 2004 |pmid= 15489336 |doi= 10.1101/gr.2576704 | pmc=528930  |name-list-format=vanc| author2=Arlt D  | author3=Huber W  | display-authors=3  | last4=Wellenreuther  | first4=R  | last5=Schleeger  | first5=S  | last6=Mehrle  | first6=A  | last7=Bechtel  | first7=S  | last8=Sauermann  | first8=M  | last9=Korf  | first9=U }}
*{{cite journal  | author=Wiemann S, Arlt D, Huber W, ''et al.'' |title=From ORFeome to biology: a functional genomics pipeline. |journal=Genome Res. |volume=14 |issue= 10B |pages= 2136-44 |year= 2004 |pmid= 15489336 |doi= 10.1101/gr.2576704 }}
*{{cite journal  | author=Gerhard DS |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  |name-list-format=vanc| author2=Wagner L  | author3=Feingold EA  | display-authors=3  | last4=Shenmen  | first4=CM  | last5=Grouse  | first5=LH  | last6=Schuler  | first6=G  | last7=Klein  | first7=SL  | last8=Old  | first8=S  | last9=Rasooly  | first9=R }}
*{{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  | author=Ota T |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 |name-list-format=vanc| author2=Suzuki Y  | author3=Nishikawa T  | display-authors=3  | last4=Otsuki  | first4=Tetsuji  | last5=Sugiyama  | first5=Tomoyasu  | last6=Irie  | first6=Ryotaro  | last7=Wakamatsu  | first7=Ai  | last8=Hayashi  | first8=Koji  | last9=Sato  | first9=Hiroyuki }}
*{{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  | author=Hillier LW |title=The DNA sequence of human chromosome 7 |journal=Nature |volume=424 |issue= 6945 |pages= 157–64 |year= 2003 |pmid= 12853948 |doi= 10.1038/nature01782 |name-list-format=vanc| author2=Fulton RS  | author3=Fulton LA  | display-authors=3  | last4=Graves  | first4=Tina A.  | last5=Pepin  | first5=Kymberlie H.  | last6=Wagner-Mcpherson  | first6=Caryn  | last7=Layman  | first7=Dan  | last8=Maas  | first8=Jason  | last9=Jaeger  | first9=Sara }}
*{{cite journal  | author=Hillier LW, Fulton RS, Fulton LA, ''et al.'' |title=The DNA sequence of human chromosome 7. |journal=Nature |volume=424 |issue= 6945 |pages= 157-64 |year= 2003 |pmid= 12853948 |doi= 10.1038/nature01782 }}
*{{cite journal  | author=Strausberg RL |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  |name-list-format=vanc| author2=Feingold EA  | author3=Grouse LH  | display-authors=3  | last4=Derge  | first4=JG  | last5=Klausner  | first5=RD  | last6=Collins  | first6=FS  | last7=Wagner  | first7=L  | last8=Shenmen  | first8=CM  | last9=Schuler  | first9=GD }}
*{{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  | author=Simpson JC |title=Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing |journal=EMBO Rep. |volume=1 |issue= 3 |pages= 287–92 |year= 2001 |pmid= 11256614 |doi= 10.1093/embo-reports/kvd058 | pmc=1083732  |name-list-format=vanc| author2=Wellenreuther R  | author3=Poustka A  | display-authors=3  | last4=Pepperkok  | first4=R  | last5=Wiemann  | first5=S }}
*{{cite journal  | author=Simpson JC, Wellenreuther R, Poustka A, ''et al.'' |title=Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing. |journal=EMBO Rep. |volume=1 |issue= 3 |pages= 287-92 |year= 2001 |pmid= 11256614 |doi= 10.1093/embo-reports/kvd058 }}
*{{cite journal  | author=Wiemann S |title=Toward a Catalog of Human Genes and Proteins: Sequencing and Analysis of 500 Novel Complete Protein Coding Human cDNAs |journal=Genome Res. |volume=11 |issue= 3 |pages= 422–35 |year= 2001 |pmid= 11230166 |doi= 10.1101/gr.GR1547R  | pmc=311072  |name-list-format=vanc| author2=Weil B  | author3=Wellenreuther R  | display-authors=3  | last4=Gassenhuber  | first4=J  | last5=Glassl  | first5=S  | last6=Ansorge  | first6=W  | last7=Böcher  | first7=M  | last8=Blöcker  | first8=H  | last9=Bauersachs  | first9=S }}
*{{cite journal  | author=Wiemann S, Weil B, Wellenreuther R, ''et al.'' |title=Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. |journal=Genome Res. |volume=11 |issue= 3 |pages= 422-35 |year= 2001 |pmid= 11230166 |doi= 10.1101/gr.154701 }}
*{{cite journal  |vauthors=Hartley JL, Temple GF, Brasch MA |title=DNA Cloning Using In Vitro Site-Specific Recombination |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788–95 |year= 2001 |pmid= 11076863 |doi=10.1101/gr.143000  | pmc=310948 }}
*{{cite journal  | author=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788-95 |year= 2001 |pmid= 11076863 |doi=  }}
*{{cite journal  | author=Lai CH |title=Identification of Novel Human Genes Evolutionarily Conserved in Caenorhabditis elegans by Comparative Proteomics |journal=Genome Res. |volume=10 |issue= 5 |pages= 703–13 |year= 2000 |pmid= 10810093 |doi=10.1101/gr.10.5.703  | pmc=310876  |name-list-format=vanc| author2=Chou CY  | author3=Ch'ang LY  | display-authors=3  | last4=Liu  | first4=CS  | last5=Lin  | first5=W }}
*{{cite journal  | author=Lai CH, Chou CY, Ch'ang LY, ''et al.'' |title=Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics. |journal=Genome Res. |volume=10 |issue= 5 |pages= 703-13 |year= 2000 |pmid= 10810093 |doi=  }}
*{{cite journal  |title=Toward a complete human genome sequence |journal=Genome Res. |volume=8 |issue= 11 |pages= 1097–108 |year= 1999 |pmid= 9847074 |doi=  10.1101/gr.8.11.1097  | author1= <Please add first missing authors to populate metadata.>}}
*{{cite journal  | author= |title=Toward a complete human genome sequence. |journal=Genome Res. |volume=8 |issue= 11 |pages= 1097-108 |year= 1999 |pmid= 9847074 |doi=  }}
}}
}}
{{refend}}
{{refend}}


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Latest revision as of 16:55, 21 July 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
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Wikidata
View/Edit Human

WD repeat domain phosphoinositide-interacting protein 2 is a protein that in humans is encoded by the WIPI2 gene.[1][2]

Function

WD40 repeat proteins are key components of many essential biologic functions. They regulate the assembly of multiprotein complexes by presenting a beta-propeller platform for simultaneous and reversible protein-protein interactions. Members of the WIPI subfamily of WD40 repeat proteins, such as WIPI2, have a 7-bladed propeller structure and contain a conserved motif for interaction with phospholipids.[1][2]

WIPI2 is the mammalian homolog of Atg18, not Atg21, along with the closely related protein, WIPI1. WIPI2 mRNA is readily detectable in several commonly used laboratory cell lines (HEK293A, HeLa, A431) and several cancer cell lines, while WIPI1 expression is limited to cancer cells.

The Atg proteins regulate autophagy, which is a lysosomal degradation pathway required for maintaining cell health, surviving periods of nutrient deprivation and also plays a role in cancer, neurodegeneration and immune responses to a diverse range of pathogens.[3] WIPI2 is recruited early to the forming autophagosome, along with DFCP-1, ULK-1 and Atg16, where it positively regulates the lipidation of Atg8 (LC3). This is not true for WIPI1.

See also

References

  1. ↑ 1.0 1.1 Proikas-Cezanne T, Waddell S, Gaugel A, Frickey T, Lupas A, Nordheim A (Dec 2004). "WIPI-1alpha (WIPI49), a member of the novel 7-bladed WIPI protein family, is aberrantly expressed in human cancer and is linked to starvation-induced autophagy". Oncogene. 23 (58): 9314–25. doi:10.1038/sj.onc.1208331. PMID 15602573.
  2. ↑ 2.0 2.1 "Entrez Gene: WIPI2 WD repeat domain, phosphoinositide interacting 2".
  3. ↑ Orsi A, Polson HE, Tooze SA (December 2009). "Membrane trafficking events that partake in autophagy". Curr Opin Cell Biol. 22 (2): 150–6. doi:10.1016/j.ceb.2009.11.013. PMID 20036114. 
* Polson HE, de Lartigue J, Rigden DJ, Reedijk M, Urbé S, Clague MJ, Tooze SA (2010). "Mammalian Atg18 (WIPI2) localizes to omegasome-anchored phagophores and positively regulates LC3 lipidation". Autophagy. 6: 506–22. doi:10.4161/auto.6.4.11863. PMID 20505359.

Further reading



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