CDCP1: Difference between revisions

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{{Infobox_gene}}
{{PBB_Controls
'''CUB domain-containing protein 1''' (CDCP1) is a [[protein]] that in humans is encoded by the ''CDCP1'' [[gene]].<ref name="pmid11466621">{{cite journal | vauthors = Scherl-Mostageer M, Sommergruber W, Abseher R, Hauptmann R, Ambros P, Schweifer N | title = Identification of a novel gene, CDCP1, overexpressed in human colorectal cancer | journal = Oncogene | volume = 20 | issue = 32 | pages = 4402–8 | date = July 2001 | pmid = 11466621 | pmc =  | doi = 10.1038/sj.onc.1204566 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: CDCP1 CUB domain containing protein 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=64866| accessdate = }}</ref> CDCP1 has also been designated as '''CD318''' ([[cluster of differentiation]] 318) and '''Trask''' (Transmembrane and associated with src kinases). [[Alternative splicing|Alternatively spliced]] transcript variants encoding distinct [[protein isoform|isoforms]] have been reported.<ref name="entrez" />
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = CUB domain containing protein 1
| HGNCid = 24357
| Symbol = CDCP1
| AltSymbols =; CD318; SIMA135; TRASK
| OMIM = 
| ECnumber = 
| Homologene = 11276
| MGIid = 2442010
| GeneAtlas_image1 = PBB_GE_CDCP1_218451_at_tn.png
| Function =  
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process =
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 64866
    | Hs_Ensembl = ENSG00000163814
    | Hs_RefseqProtein = NP_073753
    | Hs_RefseqmRNA = NM_022842
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 3
    | Hs_GenLoc_start = 45098774
    | Hs_GenLoc_end = 45162918
    | Hs_Uniprot = Q9H5V8
    | Mm_EntrezGene = 109332
    | Mm_Ensembl = ENSMUSG00000035498
    | Mm_RefseqmRNA = NM_133974
    | Mm_RefseqProtein = NP_598735
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 9
    | Mm_GenLoc_start = 123020971
    | Mm_GenLoc_end = 123064736
    | Mm_Uniprot = Q05D42
  }}
}}
'''CUB domain containing protein 1''', also known as '''CDCP1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CDCP1 CUB domain containing protein 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=64866| accessdate = }}</ref> CDCP1 has also been designated as '''CD318''' ([[cluster of differentiation]] 318).


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
CDCP1/Trask  is not important for the development of the mouse.<ref name="pmid23243018">{{cite journal | vauthors = Spassov DS, Wong CH, Wong SY, Reiter JF, Moasser MM| title = Trask loss enhances tumorigenic growth by liberating integrin signaling and growth factor receptor cross-talk in unanchored cells| journal = Cancer Research | volume = 73 | issue = 3 | pages = 1168–79 | year = 2013 | pmid = 23243018| pmc = 3563920  | doi = 10.1158/0008-5472.CAN-12-2496}}</ref> Adult mice lacking CDCP1 do not exhibit gross morphologic, reproductive or behavioral abnormalities compared with wild-type mice, and histologic examination of multiple organ systems has shown no significant pathology and no observed histologic differences.<ref name="pmid23243018"/> CDCP1 is a ligand for CD6, a receptor molecule expressed on certain T-cells and may play a role in their migration and chemotaxis. As such CDCP1 may contribute to autoimmune diseases such as encephalomyelitis, multiple sclerosis and inflammatory arthritis.<ref name="pmid28760953">{{cite journal | vauthors = Enyindah-Asonye G, Li Y, Ruth JH, Spassov DS, Hebron KE, Zijlstra A, Moasser MM, Wang B, Singer NG, Cui H, Ohara RA, Rasmussen SM, Fox DA, Lin F| title = CD318 is a ligand for CD6| journal = Proc Natl Acad Sci U S A | volume = 114 | issue = 33 | pages = E6912–E6921 | year = 2017 | pmid = 28760953| pmc = 5565428  | doi = 10.1073/pnas.1704008114}}</ref>
{{PBB_Summary
| section_title =  
| summary_text = The protein encoded by this gene is a transmembrane protein containing three extracellular CUB domains. This protein is found to be overexpressed in colon and lung cancers. Its expression level is correlated with the metastatic ability of carcinoma cells. This protein is located on the cell surface. It has been shown to be tyrosine phosphorylated in a cancer cell line. Alternatively spliced transcript variants encoding distinct isoforms have been reported.<ref name="entrez">{{cite web | title = Entrez Gene: CDCP1 CUB domain containing protein 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=64866| accessdate = }}</ref>
}}


==References==
CDCP1 is a 140 kD transmembrane [[glycoprotein]] with a large extracellular domain (ECD) containing two [[CUB domain]]s, and a smaller intracellular domain (ICD). CDCP1 is cleaved by serine proteases at the extracellular domain next to Arg368 to generate a truncated molecule of 80 kDa size.<ref name="pmid16007225">{{cite journal | vauthors = Bhatt AS, Erdjument-Bromage H, Tempst P, Craik CS, Moasser MM | title = Adhesion signaling by a novel mitotic substrate of src kinases | journal = Oncogene | volume = 24| issue = 34 | pages = 5333–43| year = 2005 | pmid = 16007225 | pmc = 3023961  | doi =  10.1038/sj.onc.1208582}}</ref> Different cell lines express different amounts of p140 and p80, depending on the activity of endogenous serine proteases. In vivo, CDCP1 is not cleaved during normal physiological circumstances, but its cleavage can be induced during tumorigenesis or tissue injury.<ref name="pmid23243018"/>
{{reflist|2}}


==Further reading==
The intracellular domain of CDCP1 contains five tyrosine residues - Y707, Y734, Y743, Y762 and Y806. Phosphorylation of CDCP1 is exclusively mediated by Src kinases and depends on the adherence state of the cells.<ref name="pmid21559459">{{cite journal | vauthors = Spassov DS, Ahuja D, Wong CH, Moasser MM | title = The structural features of Trask that mediate its anti-adhesive functions | journal = PLoS One | volume = 6 | issue = 4 | pages = e19154 | year = 2011 | pmid = 21559459 | pmc = 3084758 | doi = 10.1371/journal.pone.0019154 }}</ref><ref name="pmid19349359">{{cite journal | vauthors = Spassov DS, Baehner FL, Wong CH, McDonough S, Moasser MM | title = The transmembrane src substrate Trask is an epithelial protein that signals during anchorage deprivation | journal = Am J Pathol | volume = 174| issue = 5 | pages = 1756–65 | year = 2009 | pmid = 19349359 | pmc = 2671264  | doi =  10.2353/ajpath.2009.080890 }}</ref> The tyrosine phosphorylation of CDCP1 in cultured cells occurs when cells are induced to detach by [[trypsin]] or [[ethylenediaminetetraacetic acid|EDTA]], or seen spontaneously during [[mitosis|mitotic]] detachment. The loss of anchorage or cellular detachment is associated with the phosphorylation of CDCP1 as well as the concomitant dephosphorylation of focal adhesion proteins, consistent with the dismantling of focal adhesions.<ref name="pmid19349359"/> Contrary, during cellular attachment CDCP1 is dephosphorylated, allowing the phosphorylation of focal adhesion proteins. The anti-adhesion and anti-migratory functions of CDCP1 are mediated through negative regulation on integrin receptors.<ref name="pmid21189288">{{cite journal | vauthors = Spassov DS, Wong CH, Sergina N, Ahuja D, Fried M, Sheppard D, Moasser MM| title = Phosphorylation of Trask by Src kinases inhibits integrin clustering and functions in exclusion with focal adhesion signaling | journal = Mol Cell Biol | volume = 31| issue = 4 | pages = 766–82 | year = 2011 | pmid = 21189288 | pmc = 3028653  | doi = 10.1128/MCB.00841-10 }}</ref>
 
== Clinical significance ==
 
The phosphorylation of CDCP1 is seen in many cancers, including some pre-invasive cancers as well as in invasive tumors and in tumor metastases.<ref name="Wortmann_2009">{{cite journal | vauthors = Wortmann A, He Y, Deryugina EI, Quigley JP, Hooper JD | title = The cell surface glycoprotein CDCP1 in cancer--insights, opportunities, and challenges | journal = IUBMB Life | volume = 61 | issue = 7 | pages = 723–30 | date = July 2009 | pmid = 19514048 | doi = 10.1002/iub.198 }}</ref>
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Xia Y, Gil SG, Carter WG | title = Anchorage mediated by integrin alpha6beta4 to laminin 5 (epiligrin) regulates tyrosine phosphorylation of a membrane-associated 80-kD protein | journal = The Journal of Cell Biology | volume = 132 | issue = 4 | pages = 727–40 | date = February 1996 | pmid = 8647901 | pmc = 2199869 | doi = 10.1083/jcb.132.4.727 }}
| citations =
* {{cite journal | vauthors = Hooper JD, Zijlstra A, Aimes RT, Liang H, Claassen GF, Tarin D, Testa JE, Quigley JP | title = Subtractive immunization using highly metastatic human tumor cells identifies SIMA135/CDCP1, a 135 kDa cell surface phosphorylated glycoprotein antigen | journal = Oncogene | volume = 22 | issue = 12 | pages = 1783–94 | date = March 2003 | pmid = 12660814 | doi = 10.1038/sj.onc.1206220 }}
*{{cite journal | author=Xia Y, Gil SG, Carter WG |title=Anchorage mediated by integrin alpha6beta4 to laminin 5 (epiligrin) regulates tyrosine phosphorylation of a membrane-associated 80-kD protein. |journal=J. Cell Biol. |volume=132 |issue= 4 |pages= 727-40 |year= 1996 |pmid= 8647901 |doi= }}
* {{cite journal | vauthors = Conze T, Lammers R, Kuci S, Scherl-Mostageer M, Schweifer N, Kanz L, Buhring HJ | title = CDCP1 is a novel marker for hematopoietic stem cells | journal = Annals of the New York Academy of Sciences | volume = 996 | issue = 1 | pages = 222–6 | date = May 2003 | pmid = 12799299 | doi = 10.1111/j.1749-6632.2003.tb03249.x }}
*{{cite journal  | author=Scherl-Mostageer M, Sommergruber W, Abseher R, ''et al.'' |title=Identification of a novel gene, CDCP1, overexpressed in human colorectal cancer. |journal=Oncogene |volume=20 |issue= 32 |pages= 4402-8 |year= 2001 |pmid= 11466621 |doi= }}
* {{cite journal | vauthors = Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A | title = The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment | journal = Genome Research | volume = 13 | issue = 10 | pages = 2265–70 | date = October 2003 | pmid = 12975309 | pmc = 403697 | doi = 10.1101/gr.1293003 }}
*{{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 = Brown TA, Yang TM, Zaitsevskaia T, Xia Y, Dunn CA, Sigle RO, Knudsen B, Carter WG | title = Adhesion or plasmin regulates tyrosine phosphorylation of a novel membrane glycoprotein p80/gp140/CUB domain-containing protein 1 in epithelia | journal = The Journal of Biological Chemistry | volume = 279 | issue = 15 | pages = 14772–83 | date = April 2004 | pmid = 14739293 | doi = 10.1074/jbc.M309678200 }}
*{{cite journal | author=Hooper JD, Zijlstra A, Aimes RT, ''et al.'' |title=Subtractive immunization using highly metastatic human tumor cells identifies SIMA135/CDCP1, a 135 kDa cell surface phosphorylated glycoprotein antigen. |journal=Oncogene |volume=22 |issue= 12 |pages= 1783-94 |year= 2003 |pmid= 12660814 |doi= 10.1038/sj.onc.1206220 }}
* {{cite journal | vauthors = Bühring HJ, Kuçi S, Conze T, Rathke G, Bartolović K, Grünebach F, Scherl-Mostageer M, Brümmendorf TH, Schweifer N, Lammers R | title = CDCP1 identifies a broad spectrum of normal and malignant stem/progenitor cell subsets of hematopoietic and nonhematopoietic origin | journal = Stem Cells | volume = 22 | issue = 3 | pages = 334–43 | year = 2005 | pmid = 15153610 | doi = 10.1634/stemcells.22-3-334 }}
*{{cite journal | author=Conze T, Lammers R, Kuci S, ''et al.'' |title=CDCP1 is a novel marker for hematopoietic stem cells. |journal=Ann. N. Y. Acad. Sci. |volume=996 |issue= |pages= 222-6 |year= 2003 |pmid= 12799299 |doi= }}
* {{cite journal | vauthors = Benes CH, Wu N, Elia AE, Dharia T, Cantley LC, Soltoff SP | title = The C2 domain of PKCdelta is a phosphotyrosine binding domain | journal = Cell | volume = 121 | issue = 2 | pages = 271–80 | date = April 2005 | pmid = 15851033 | doi = 10.1016/j.cell.2005.02.019 }}
*{{cite journal | author=Clark HF, Gurney AL, Abaya E, ''et al.'' |title=The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. |journal=Genome Res. |volume=13 |issue= 10 |pages= 2265-70 |year= 2003 |pmid= 12975309 |doi= 10.1101/gr.1293003 }}
* {{cite journal | vauthors = Bhatt AS, Erdjument-Bromage H, Tempst P, Craik CS, Moasser MM | title = Adhesion signaling by a novel mitotic substrate of src kinases | journal = Oncogene | volume = 24 | issue = 34 | pages = 5333–43 | date = August 2005 | pmid = 16007225 | pmc = 3023961 | doi = 10.1038/sj.onc.1208582 }}
*{{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 = André M, Le Caer JP, Greco C, Planchon S, El Nemer W, Boucheix C, Rubinstein E, Chamot-Rooke J, Le Naour F | title = Proteomic analysis of the tetraspanin web using LC-ESI-MS/MS and MALDI-FTICR-MS | journal = Proteomics | volume = 6 | issue = 5 | pages = 1437–49 | date = March 2006 | pmid = 16404722 | doi = 10.1002/pmic.200500180 }}
*{{cite journal  | author=Brown TA, Yang TM, Zaitsevskaia T, ''et al.'' |title=Adhesion or plasmin regulates tyrosine phosphorylation of a novel membrane glycoprotein p80/gp140/CUB domain-containing protein 1 in epithelia. |journal=J. Biol. Chem. |volume=279 |issue= 15 |pages= 14772-83 |year= 2004 |pmid= 14739293 |doi= 10.1074/jbc.M309678200 }}
* {{cite journal | vauthors = Kimura H, Morii E, Ikeda JI, Ezoe S, Xu JX, Nakamichi N, Tomita Y, Shibayama H, Kanakura Y, Aozasa K | title = Role of DNA methylation for expression of novel stem cell marker CDCP1 in hematopoietic cells | journal = Leukemia | volume = 20 | issue = 9 | pages = 1551–6 | date = September 2006 | pmid = 16926850 | doi = 10.1038/sj.leu.2404312 }}
*{{cite journal | author=Bühring HJ, Kuçi S, Conze T, ''et al.'' |title=CDCP1 identifies a broad spectrum of normal and malignant stem/progenitor cell subsets of hematopoietic and nonhematopoietic origin. |journal=Stem Cells |volume=22 |issue= 3 |pages= 334-43 |year= 2005 |pmid= 15153610 |doi=  }}
* {{cite journal | vauthors = Perry SE, Robinson P, Melcher A, Quirke P, Bühring HJ, Cook GP, Blair GE | title = Expression of the CUB domain containing protein 1 (CDCP1) gene in colorectal tumour cells | journal = FEBS Letters | volume = 581 | issue = 6 | pages = 1137–42 | date = March 2007 | pmid = 17335815 | doi = 10.1016/j.febslet.2007.02.025 }}
*{{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 = Uekita T, Jia L, Narisawa-Saito M, Yokota J, Kiyono T, Sakai R | title = CUB domain-containing protein 1 is a novel regulator of anoikis resistance in lung adenocarcinoma | journal = Molecular and Cellular Biology | volume = 27 | issue = 21 | pages = 7649–60 | date = November 2007 | pmid = 17785447 | pmc = 2169043 | doi = 10.1128/MCB.01246-07 }}
*{{cite journal | author=Benes CH, Wu N, Elia AE, ''et al.'' |title=The C2 domain of PKCdelta is a phosphotyrosine binding domain. |journal=Cell |volume=121 |issue= 2 |pages= 271-80 |year= 2005 |pmid= 15851033 |doi= 10.1016/j.cell.2005.02.019 }}
*{{cite journal | author=Bhatt AS, Erdjument-Bromage H, Tempst P, ''et al.'' |title=Adhesion signaling by a novel mitotic substrate of src kinases. |journal=Oncogene |volume=24 |issue= 34 |pages= 5333-43 |year= 2005 |pmid= 16007225 |doi= 10.1038/sj.onc.1208582 }}
*{{cite journal | author=André M, Le Caer JP, Greco C, ''et al.'' |title=Proteomic analysis of the tetraspanin web using LC-ESI-MS/MS and MALDI-FTICR-MS. |journal=Proteomics |volume=6 |issue= 5 |pages= 1437-49 |year= 2006 |pmid= 16404722 |doi= 10.1002/pmic.200500180 }}
*{{cite journal | author=Kimura H, Morii E, Ikeda JI, ''et al.'' |title=Role of DNA methylation for expression of novel stem cell marker CDCP1 in hematopoietic cells. |journal=Leukemia |volume=20 |issue= 9 |pages= 1551-6 |year= 2006 |pmid= 16926850 |doi= 10.1038/sj.leu.2404312 }}
*{{cite journal | author=Perry SE, Robinson P, Melcher A, ''et al.'' |title=Expression of the CUB domain containing protein 1 (CDCP1) gene in colorectal tumour cells. |journal=FEBS Lett. |volume=581 |issue= 6 |pages= 1137-42 |year= 2007 |pmid= 17335815 |doi= 10.1016/j.febslet.2007.02.025 }}
*{{cite journal | author=Uekita T, Jia L, Narisawa-Saito M, ''et al.'' |title=CUB domain-containing protein 1 is a novel regulator of anoikis resistance in lung adenocarcinoma. |journal=Mol. Cell. Biol. |volume=27 |issue= 21 |pages= 7649-60 |year= 2007 |pmid= 17785447 |doi= 10.1128/MCB.01246-07 }}
}}
{{refend}}
{{refend}}


==External links==
== External links ==
* {{MeshName|CDCP1+protein,+human}}
* {{MeshName|CDCP1+protein,+human}}
* {{UCSC gene info|CDCP1}}


{{membrane-protein-stub}}
{{NLM content}}
{{NLM content}}
{{Clusters of differentiation}}
{{Clusters of differentiation}}
[[Category:Clusters of differentiation]]
[[Category:Clusters of differentiation]]
{{WikiDoc Sources}}
 
 
{{membrane-protein-stub}}

Latest revision as of 03:02, 15 January 2019

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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
PubMed searchn/an/a
Wikidata
View/Edit Human

CUB domain-containing protein 1 (CDCP1) is a protein that in humans is encoded by the CDCP1 gene.[1][2] CDCP1 has also been designated as CD318 (cluster of differentiation 318) and Trask (Transmembrane and associated with src kinases). Alternatively spliced transcript variants encoding distinct isoforms have been reported.[2]

Function

CDCP1/Trask is not important for the development of the mouse.[3] Adult mice lacking CDCP1 do not exhibit gross morphologic, reproductive or behavioral abnormalities compared with wild-type mice, and histologic examination of multiple organ systems has shown no significant pathology and no observed histologic differences.[3] CDCP1 is a ligand for CD6, a receptor molecule expressed on certain T-cells and may play a role in their migration and chemotaxis. As such CDCP1 may contribute to autoimmune diseases such as encephalomyelitis, multiple sclerosis and inflammatory arthritis.[4]

CDCP1 is a 140 kD transmembrane glycoprotein with a large extracellular domain (ECD) containing two CUB domains, and a smaller intracellular domain (ICD). CDCP1 is cleaved by serine proteases at the extracellular domain next to Arg368 to generate a truncated molecule of 80 kDa size.[5] Different cell lines express different amounts of p140 and p80, depending on the activity of endogenous serine proteases. In vivo, CDCP1 is not cleaved during normal physiological circumstances, but its cleavage can be induced during tumorigenesis or tissue injury.[3]

The intracellular domain of CDCP1 contains five tyrosine residues - Y707, Y734, Y743, Y762 and Y806. Phosphorylation of CDCP1 is exclusively mediated by Src kinases and depends on the adherence state of the cells.[6][7] The tyrosine phosphorylation of CDCP1 in cultured cells occurs when cells are induced to detach by trypsin or EDTA, or seen spontaneously during mitotic detachment. The loss of anchorage or cellular detachment is associated with the phosphorylation of CDCP1 as well as the concomitant dephosphorylation of focal adhesion proteins, consistent with the dismantling of focal adhesions.[7] Contrary, during cellular attachment CDCP1 is dephosphorylated, allowing the phosphorylation of focal adhesion proteins. The anti-adhesion and anti-migratory functions of CDCP1 are mediated through negative regulation on integrin receptors.[8]

Clinical significance

The phosphorylation of CDCP1 is seen in many cancers, including some pre-invasive cancers as well as in invasive tumors and in tumor metastases.[9]

References

  1. ↑ Scherl-Mostageer M, Sommergruber W, Abseher R, Hauptmann R, Ambros P, Schweifer N (July 2001). "Identification of a novel gene, CDCP1, overexpressed in human colorectal cancer". Oncogene. 20 (32): 4402–8. doi:10.1038/sj.onc.1204566. PMID 11466621.
  2. ↑ 2.0 2.1 "Entrez Gene: CDCP1 CUB domain containing protein 1".
  3. ↑ 3.0 3.1 3.2 Spassov DS, Wong CH, Wong SY, Reiter JF, Moasser MM (2013). "Trask loss enhances tumorigenic growth by liberating integrin signaling and growth factor receptor cross-talk in unanchored cells". Cancer Research. 73 (3): 1168–79. doi:10.1158/0008-5472.CAN-12-2496. PMC 3563920. PMID 23243018.
  4. ↑ Enyindah-Asonye G, Li Y, Ruth JH, Spassov DS, Hebron KE, Zijlstra A, Moasser MM, Wang B, Singer NG, Cui H, Ohara RA, Rasmussen SM, Fox DA, Lin F (2017). "CD318 is a ligand for CD6". Proc Natl Acad Sci U S A. 114 (33): E6912–E6921. doi:10.1073/pnas.1704008114. PMC 5565428. PMID 28760953.
  5. ↑ Bhatt AS, Erdjument-Bromage H, Tempst P, Craik CS, Moasser MM (2005). "Adhesion signaling by a novel mitotic substrate of src kinases". Oncogene. 24 (34): 5333–43. doi:10.1038/sj.onc.1208582. PMC 3023961. PMID 16007225.
  6. ↑ Spassov DS, Ahuja D, Wong CH, Moasser MM (2011). "The structural features of Trask that mediate its anti-adhesive functions". PLoS One. 6 (4): e19154. doi:10.1371/journal.pone.0019154. PMC 3084758. PMID 21559459.
  7. ↑ 7.0 7.1 Spassov DS, Baehner FL, Wong CH, McDonough S, Moasser MM (2009). "The transmembrane src substrate Trask is an epithelial protein that signals during anchorage deprivation". Am J Pathol. 174 (5): 1756–65. doi:10.2353/ajpath.2009.080890. PMC 2671264. PMID 19349359.
  8. ↑ Spassov DS, Wong CH, Sergina N, Ahuja D, Fried M, Sheppard D, Moasser MM (2011). "Phosphorylation of Trask by Src kinases inhibits integrin clustering and functions in exclusion with focal adhesion signaling". Mol Cell Biol. 31 (4): 766–82. doi:10.1128/MCB.00841-10. PMC 3028653. PMID 21189288.
  9. ↑ Wortmann A, He Y, Deryugina EI, Quigley JP, Hooper JD (July 2009). "The cell surface glycoprotein CDCP1 in cancer--insights, opportunities, and challenges". IUBMB Life. 61 (7): 723–30. doi:10.1002/iub.198. PMID 19514048.

Further reading

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.


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