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Missense mutations in the PTPN11 locus are associated with both [[Noonan syndrome]] and [[Leopard syndrome]]. At least 79 disease-causing mutations in this gene have been discovered.<ref name = "Šimčíková_2019 - supplementary table S7">{{cite journal | vauthors = Šimčíková D, Heneberg P | title = Refinement of evolutionary medicine predictions based on clinical evidence for the manifestations of Mendelian diseases | journal = Scientific Reports | volume = 9 | issue = 1 | pages = 18577 | date = December 2019 | pmid = 31819097 | pmc = 6901466 | doi = 10.1038/s41598-019-54976-4| bibcode = 2019NatSR...918577S }}</ref>
Missense mutations in the PTPN11 locus are associated with both [[Noonan syndrome]] and [[Leopard syndrome]]. At least 79 disease-causing mutations in this gene have been discovered.<ref name = "Šimčíková_2019 - supplementary table S7">{{cite journal | vauthors = Šimčíková D, Heneberg P | title = Refinement of evolutionary medicine predictions based on clinical evidence for the manifestations of Mendelian diseases | journal = Scientific Reports | volume = 9 | issue = 1 | pages = 18577 | date = December 2019 | pmid = 31819097 | pmc = 6901466 | doi = 10.1038/s41598-019-54976-4| bibcode = 2019NatSR...918577S }}</ref>


It has also been associated with [[Metachondromatosis]].<ref name="pmid20577567">{{cite journal | vauthors = Sobreira NL, Cirulli ET, Avramopoulos D, Wohler E, Oswald GL, Stevens EL, Ge D, Shianna KV, Smith JP, Maia JM, Gumbs CE, Pevsner J, Thomas G, Valle D, Hoover-Fong JE, Goldstein DB | title = Whole-genome sequencing of a single proband together with linkage analysis identifies a Mendelian disease gene | journal = PLOS Genet. | volume = 6 | issue = 6 | pages = e1000991 | date = June 2010 | pmid = 20577567 | pmc = 2887469 | doi = 10.1371/journal.pgen.1000991 | doi-access = free }}</ref>
It has also been associated with [[metachondromatosis]].<ref name="pmid20577567">{{cite journal | vauthors = Sobreira NL, Cirulli ET, Avramopoulos D, Wohler E, Oswald GL, Stevens EL, Ge D, Shianna KV, Smith JP, Maia JM, Gumbs CE, Pevsner J, Thomas G, Valle D, Hoover-Fong JE, Goldstein DB | title = Whole-genome sequencing of a single proband together with linkage analysis identifies a Mendelian disease gene | journal = PLOS Genet. | volume = 6 | issue = 6 | pages = e1000991 | date = June 2010 | pmid = 20577567 | pmc = 2887469 | doi = 10.1371/journal.pgen.1000991 | doi-access = free }}</ref>


===Noonan syndrome===
===Noonan syndrome===
Line 25: Line 25:


==Cancer associated with PTPN11==
==Cancer associated with PTPN11==
Patients with a subset of Noonan syndrome PTPN11 mutations also have a higher prevalence of [[juvenile myelomonocytic leukemia]]s (JMML). Activating Shp2 mutations have also been detected in [[neuroblastoma]], [[melanoma]], [[acute myeloid leukemia]], [[breast cancer]], [[lung cancer]], [[colorectal cancer]].<ref name="pmid15604238">{{cite journal | vauthors = Bentires-Alj M, Paez JG, David FS, Keilhack H, Halmos B, Naoki K, Maris JM, Richardson A, Bardelli A, Sugarbaker DJ, Richards WG, Du J, Girard L, Minna JD, Loh ML, Fisher DE, Velculescu VE, Vogelstein B, Meyerson M, Sellers WR, Neel BG | title = Activating mutations of the noonan syndrome-associated SHP2/PTPN11 gene in human solid tumors and adult acute myelogenous leukemia | journal = Cancer Res. | volume = 64 | issue = 24 | pages = 8816–20 | date = December 2004 | pmid = 15604238 | doi = 10.1158/0008-5472.CAN-04-1923 | doi-access = free }}</ref> Recently, a relatively high prevalence of PTPN11 mutations (24%) were detected by [[next-generation sequencing]] in a cohort of [[NPM1]]-mutated [[acute myeloid leukemia]] patients,<ref>{{cite journal | vauthors = Patel SS, Kuo FC, Gibson CJ, Steensma DP, Soiffer RJ, Alyea EP, Chen YA, Fathi AT, Graubert TA, Brunner AM, Wadleigh M, Stone RM, DeAngelo DJ, Nardi V, Hasserjian RP, Weinberg OK | title = High NPM1 mutant allele burden at diagnosis predicts unfavorable outcomes in de novo AML | journal = Blood | volume = 131 | issue = 25 | pages = 2816–2825 | date = May 2018 | pmid = 29724895 | pmc = 6265642 | doi = 10.1182/blood-2018-01-828467 }}</ref> although the prognostic significance of such associations has not been clarified. These data suggests that Shp2 may be a [[proto-oncogene]]. However, it has been reported that PTPN11/Shp2 can act as either tumor [[Proto-oncogene|promoter]] or [[Tumor suppressor gene|suppressor]].<ref name="Gen-Sheng Feng"/> In aged mouse model, hepatocyte-specific deletion of PTPN11/Shp2 promotes inflammatory signaling through the [[STAT3]] pathway and hepatic inflammation/[[necrosis]], resulting in regenerative hyperplasia and spontaneous development of tumors. Decreased PTPN11/Shp2 expression was detected in a subfraction of human [[hepatocellular carcinoma|hepatocellular carcinoma (HCC)]] specimens.<ref name="Gen-Sheng Feng">{{cite journal | vauthors = Bard-Chapeau EA, Li S, Ding J, Zhang SS, Zhu HH, Princen F, Fang DD, Han T, Bailly-Maitre B, Poli V, Varki NM, Wang H, Feng GS | title = Ptpn11/Shp2 acts as a tumor suppressor in hepatocellular carcinogenesis | journal = Cancer Cell | volume = 19 | issue = 5 | pages = 629–39 | date = May 2011 | pmid = 21575863 | pmc = 3098128 | doi = 10.1016/j.ccr.2011.03.023 }}</ref> The bacterium ''[[Helicobacter pylori]]'' has been associated with gastric cancer, and this is thought to be mediated in part by the interaction of its virulence factor [[CagA]] with SHP2.<ref name="pmid16367902">{{cite journal | vauthors = Hatakeyama M, Higashi H | title = Helicobacter pylori CagA: a new paradigm for bacterial carcinogenesis | journal = Cancer Science | volume = 96 | issue = 12 | pages = 835–843 | year = 2005 | pmid = 16367902 | doi = 10.1111/j.1349-7006.2005.00130.x | s2cid = 5721063 | doi-access = free }}</ref>
Patients with a subset of Noonan syndrome PTPN11 mutations also have a higher prevalence of [[juvenile myelomonocytic leukemia]]s (JMML). Activating Shp2 mutations have also been detected in [[neuroblastoma]], [[melanoma]], [[acute myeloid leukemia]], [[breast cancer]], [[lung cancer]], [[colorectal cancer]].<ref name="pmid15604238">{{cite journal | vauthors = Bentires-Alj M, Paez JG, David FS, Keilhack H, Halmos B, Naoki K, Maris JM, Richardson A, Bardelli A, Sugarbaker DJ, Richards WG, Du J, Girard L, Minna JD, Loh ML, Fisher DE, Velculescu VE, Vogelstein B, Meyerson M, Sellers WR, Neel BG | title = Activating mutations of the noonan syndrome-associated SHP2/PTPN11 gene in human solid tumors and adult acute myelogenous leukemia | journal = Cancer Res. | volume = 64 | issue = 24 | pages = 8816–20 | date = December 2004 | pmid = 15604238 | doi = 10.1158/0008-5472.CAN-04-1923 | doi-access = free }}</ref> Recently, a relatively high prevalence of PTPN11 mutations (24%) were detected by [[next-generation sequencing]] in a cohort of [[NPM1]]-mutated [[acute myeloid leukemia]] patients,<ref>{{cite journal | vauthors = Patel SS, Kuo FC, Gibson CJ, Steensma DP, Soiffer RJ, Alyea EP, Chen YA, Fathi AT, Graubert TA, Brunner AM, Wadleigh M, Stone RM, DeAngelo DJ, Nardi V, Hasserjian RP, Weinberg OK | title = High NPM1 mutant allele burden at diagnosis predicts unfavorable outcomes in de novo AML | journal = Blood | volume = 131 | issue = 25 | pages = 2816–2825 | date = May 2018 | pmid = 29724895 | pmc = 6265642 | doi = 10.1182/blood-2018-01-828467 }}</ref> although the prognostic significance of such associations has not been clarified. These data suggests that Shp2 may be a [[proto-oncogene]]. However, it has been reported that PTPN11/Shp2 can act as either tumor [[Proto-oncogene|promoter]] or [[Tumor suppressor gene|suppressor]].<ref name="Gen-Sheng Feng"/> In aged mouse model, hepatocyte-specific deletion of PTPN11/Shp2 promotes inflammatory signaling through the [[STAT3]] pathway and hepatic inflammation/[[necrosis]], resulting in regenerative hyperplasia and spontaneous development of tumors. Decreased PTPN11/Shp2 expression was detected in a subfraction of human [[hepatocellular carcinoma]] (HCC) specimens.<ref name="Gen-Sheng Feng">{{cite journal | vauthors = Bard-Chapeau EA, Li S, Ding J, Zhang SS, Zhu HH, Princen F, Fang DD, Han T, Bailly-Maitre B, Poli V, Varki NM, Wang H, Feng GS | title = Ptpn11/Shp2 acts as a tumor suppressor in hepatocellular carcinogenesis | journal = Cancer Cell | volume = 19 | issue = 5 | pages = 629–39 | date = May 2011 | pmid = 21575863 | pmc = 3098128 | doi = 10.1016/j.ccr.2011.03.023 }}</ref> The bacterium ''[[Helicobacter pylori]]'' has been associated with gastric cancer, and this is thought to be mediated in part by the interaction of its virulence factor [[CagA]] with SHP2.<ref name="pmid16367902">{{cite journal | vauthors = Hatakeyama M, Higashi H | title = Helicobacter pylori CagA: a new paradigm for bacterial carcinogenesis | journal = Cancer Science | volume = 96 | issue = 12 | pages = 835–843 | year = 2005 | pmid = 16367902 | doi = 10.1111/j.1349-7006.2005.00130.x | s2cid = 5721063 | doi-access = free | pmc = 11159386 }}</ref>


== Interactions ==
== Interactions ==
Line 66: Line 66:


===H Pylori CagA virulence factor===
===H Pylori CagA virulence factor===
CagA is a protein and [[virulence factor]] inserted by ''[[Helicobacter pylori]]'' into gastric epithelia. Once activated by SRC phosphorylation, CagA binds to SHP2, allosterically activating it. This leads to morphological changes, abnormal mitogenic signals and sustained activity can result in [[apoptosis]] of the host cell. Epidemiological studies have shown roles of cagA- positive ''H. pylori'' in the development of [[atrophic gastritis]], [[peptic ulcer]] disease and [[stomach cancer|gastric carcinoma]].<ref name="pmid15343275">{{cite journal | vauthors = Hatakeyama M | title = Oncogenic mechanisms of the Helicobacter pylori CagA protein | journal = Nature Reviews Cancer | volume = 4 | issue = 9 | pages = 688–94 | date = September 2004 | pmid = 15343275 | doi = 10.1038/nrc1433 | s2cid = 1218835 }}</ref>
CagA is a protein and [[virulence factor]] inserted by ''[[Helicobacter pylori]]'' into gastric epithelia. Once activated by SRC phosphorylation, CagA binds to SHP2, allosterically activating it. This leads to morphological changes, abnormal mitogenic signals and sustained activity can result in [[apoptosis]] of the host cell. Epidemiological studies have shown roles of cagA- positive ''H.&nbsp;pylori'' in the development of [[atrophic gastritis]], [[peptic ulcer]] disease and [[stomach cancer|gastric carcinoma]].<ref name="pmid15343275">{{cite journal | vauthors = Hatakeyama M | title = Oncogenic mechanisms of the Helicobacter pylori CagA protein | journal = Nature Reviews Cancer | volume = 4 | issue = 9 | pages = 688–94 | date = September 2004 | pmid = 15343275 | doi = 10.1038/nrc1433 | s2cid = 1218835 }}</ref>


== References ==
== References ==
Line 80: Line 80:
* {{cite journal | vauthors = Ogata T, Yoshida R | title = PTPN11 mutations and genotype-phenotype correlations in Noonan and LEOPARD syndromes. | journal = Pediatric Endocrinology Reviews | volume = 2 | issue = 4 | pages = 669–74 | year = 2006 | pmid = 16208280 }}
* {{cite journal | vauthors = Ogata T, Yoshida R | title = PTPN11 mutations and genotype-phenotype correlations in Noonan and LEOPARD syndromes. | journal = Pediatric Endocrinology Reviews | volume = 2 | issue = 4 | pages = 669–74 | year = 2006 | pmid = 16208280 }}
* {{cite journal | vauthors = Feng GS | title = Shp2-mediated molecular signaling in control of embryonic stem cell self-renewal and differentiation. | journal = Cell Res. | volume = 17 | issue = 1 | pages = 37–41 | year = 2007 | pmid = 17211446 | doi = 10.1038/sj.cr.7310140 | doi-access = free }}
* {{cite journal | vauthors = Feng GS | title = Shp2-mediated molecular signaling in control of embryonic stem cell self-renewal and differentiation. | journal = Cell Res. | volume = 17 | issue = 1 | pages = 37–41 | year = 2007 | pmid = 17211446 | doi = 10.1038/sj.cr.7310140 | doi-access = free }}
* {{cite journal | vauthors = Edouard T, Montagner A, Dance M, Conte F, Yart A, Parfait B, Tauber M, Salles JP, Raynal P | title = How do Shp2 mutations that oppositely influence its biochemical activity result in syndromes with overlapping symptoms? | journal = Cell. Mol. Life Sci. | volume = 64 | issue = 13 | pages = 1585–90 | year = 2007 | pmid = 17453145 | doi = 10.1007/s00018-007-6509-0 | s2cid = 25934330 }}
* {{cite journal | vauthors = Edouard T, Montagner A, Dance M, Conte F, Yart A, Parfait B, Tauber M, Salles JP, Raynal P | title = How do Shp2 mutations that oppositely influence its biochemical activity result in syndromes with overlapping symptoms? | journal = Cell. Mol. Life Sci. | volume = 64 | issue = 13 | pages = 1585–90 | year = 2007 | pmid = 17453145 | doi = 10.1007/s00018-007-6509-0 | s2cid = 25934330 | pmc = 11136329 }}
{{Refend}}
{{Refend}}


Latest revision as of 05:41, 17 June 2024

PTPN11
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesPTPN11, BPTP3, CFC, JMML, METCDS, NS1, PTP-1D, PTP2C, SH-PTP2, SH-PTP3, SHP2, protein tyrosine phosphatase, non-receptor type 11, protein tyrosine phosphatase non-receptor type 11
External IDsOMIM: 176876; MGI: 99511; HomoloGene: 2122; GeneCards: PTPN11; OMA:PTPN11 - orthologs
Orthologs
SpeciesHumanMouse
Entrez

5781

19247

Ensembl

ENSG00000179295

ENSMUSG00000043733

UniProt

Q06124

P35235

RefSeq (mRNA)

NM_002834
NM_080601
NM_001330437
NM_001374625
NM_018508

NM_001109992
NM_011202

RefSeq (protein)

NP_001317366
NP_002825
NP_542168
NP_001361554

NP_001103462
NP_035332

Location (UCSC)Chr 12: 112.42 – 112.51 MbChr 5: 121.27 – 121.33 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) also known as protein-tyrosine phosphatase 1D (PTP-1D), Src homology region 2 domain-containing phosphatase-2 (SHP-2), or protein-tyrosine phosphatase 2C (PTP-2C) is an enzyme that in humans is encoded by the PTPN11 gene. PTPN11 is a protein tyrosine phosphatase (PTP) Shp2.[5][6]

PTPN11 is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP contains two tandem Src homology-2 domains, which function as phospho-tyrosine binding domains and mediate the interaction of this PTP with its substrates. This PTP is widely expressed in most tissues and plays a regulatory role in various cell signaling events that are important for a diversity of cell functions, such as mitogenic activation, metabolic control, transcription regulation, and cell migration. Mutations in this gene are a cause of Noonan syndrome as well as acute myeloid leukemia.[7]

Structure and function

[edit]

This phosphatase, along with its paralogue, Shp1, possesses a domain structure that consists of two tandem SH2 domains in its N-terminus followed by a protein tyrosine phosphatase (PTP) domain. In the inactive state, the N-terminal SH2 domain binds the PTP domain and blocks access of potential substrates to the active site. Thus, Shp2 is auto-inhibited.

Upon binding to target phospho-tyrosyl residues, the N-terminal SH2 domain is released from the PTP domain, catalytically activating the enzyme by relieving this auto-inhibition.

Genetic diseases associated with PTPN11

[edit]

Missense mutations in the PTPN11 locus are associated with both Noonan syndrome and Leopard syndrome. At least 79 disease-causing mutations in this gene have been discovered.[8]

It has also been associated with metachondromatosis.[9]

Noonan syndrome

[edit]

In the case of Noonan syndrome, mutations are broadly distributed throughout the coding region of the gene but all appear to result in hyper-activated, or unregulated mutant forms of the protein. Most of these mutations disrupt the binding interface between the N-SH2 domain and catalytic core necessary for the enzyme to maintain its auto-inhibited conformation.[10]

Leopard syndrome

[edit]

The mutations that cause Leopard syndrome are restricted regions affecting the catalytic core of the enzyme producing catalytically impaired Shp2 variants.[11] It is currently unclear how mutations that give rise to mutant variants of Shp2 with biochemically opposite characteristics result in similar human genetic syndromes.

Cancer associated with PTPN11

[edit]

Patients with a subset of Noonan syndrome PTPN11 mutations also have a higher prevalence of juvenile myelomonocytic leukemias (JMML). Activating Shp2 mutations have also been detected in neuroblastoma, melanoma, acute myeloid leukemia, breast cancer, lung cancer, colorectal cancer.[12] Recently, a relatively high prevalence of PTPN11 mutations (24%) were detected by next-generation sequencing in a cohort of NPM1-mutated acute myeloid leukemia patients,[13] although the prognostic significance of such associations has not been clarified. These data suggests that Shp2 may be a proto-oncogene. However, it has been reported that PTPN11/Shp2 can act as either tumor promoter or suppressor.[14] In aged mouse model, hepatocyte-specific deletion of PTPN11/Shp2 promotes inflammatory signaling through the STAT3 pathway and hepatic inflammation/necrosis, resulting in regenerative hyperplasia and spontaneous development of tumors. Decreased PTPN11/Shp2 expression was detected in a subfraction of human hepatocellular carcinoma (HCC) specimens.[14] The bacterium Helicobacter pylori has been associated with gastric cancer, and this is thought to be mediated in part by the interaction of its virulence factor CagA with SHP2.[15]

Interactions

[edit]

PTPN11 has been shown to interact with

H Pylori CagA virulence factor

[edit]

CagA is a protein and virulence factor inserted by Helicobacter pylori into gastric epithelia. Once activated by SRC phosphorylation, CagA binds to SHP2, allosterically activating it. This leads to morphological changes, abnormal mitogenic signals and sustained activity can result in apoptosis of the host cell. Epidemiological studies have shown roles of cagA- positive H. pylori in the development of atrophic gastritis, peptic ulcer disease and gastric carcinoma.[71]

References

[edit]
  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000179295 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000043733 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Jamieson CR, van der Burgt I, Brady AF, van Reen M, Elsawi MM, Hol F, Jeffery S, Patton MA, Mariman E (December 1994). "Mapping a gene for Noonan syndrome to the long arm of chromosome 12". Nat. Genet. 8 (4): 357–60. doi:10.1038/ng1294-357. PMID 7894486. S2CID 1582162.
  6. ^ Freeman RM, Plutzky J, Neel BG (December 1992). "Identification of a human Src homology 2-containing protein-tyrosine-phosphatase: a putative homolog of Drosophila corkscrew". Proc. Natl. Acad. Sci. U.S.A. 89 (23): 11239–43. Bibcode:1992PNAS...8911239F. doi:10.1073/pnas.89.23.11239. PMC 50525. PMID 1280823.
  7. ^ "Entrez Gene: PTPN11 protein tyrosine phosphatase, non-receptor type 11 (Noonan syndrome 1)".
  8. ^ Šimčíková D, Heneberg P (December 2019). "Refinement of evolutionary medicine predictions based on clinical evidence for the manifestations of Mendelian diseases". Scientific Reports. 9 (1): 18577. Bibcode:2019NatSR...918577S. doi:10.1038/s41598-019-54976-4. PMC 6901466. PMID 31819097.
  9. ^ Sobreira NL, Cirulli ET, Avramopoulos D, Wohler E, Oswald GL, Stevens EL, Ge D, Shianna KV, Smith JP, Maia JM, Gumbs CE, Pevsner J, Thomas G, Valle D, Hoover-Fong JE, Goldstein DB (June 2010). "Whole-genome sequencing of a single proband together with linkage analysis identifies a Mendelian disease gene". PLOS Genet. 6 (6): e1000991. doi:10.1371/journal.pgen.1000991. PMC 2887469. PMID 20577567.
  10. ^ Roberts AE, Araki T, Swanson KD, Montgomery KT, Schiripo TA, Joshi VA, Li L, Yassin Y, Tamburino AM, Neel BG, Kucherlapati RS (January 2007). "Germline gain-of-function mutations in SOS1 cause Noonan syndrome". Nat. Genet. 39 (1): 70–4. doi:10.1038/ng1926. PMID 17143285. S2CID 10222262.
  11. ^ Kontaridis MI, Swanson KD, David FS, Barford D, Neel BG (March 2006). "PTPN11 (Shp2) mutations in LEOPARD syndrome have dominant negative, not activating, effects". J. Biol. Chem. 281 (10): 6785–92. doi:10.1074/jbc.M513068200. PMID 16377799.
  12. ^ Bentires-Alj M, Paez JG, David FS, Keilhack H, Halmos B, Naoki K, Maris JM, Richardson A, Bardelli A, Sugarbaker DJ, Richards WG, Du J, Girard L, Minna JD, Loh ML, Fisher DE, Velculescu VE, Vogelstein B, Meyerson M, Sellers WR, Neel BG (December 2004). "Activating mutations of the noonan syndrome-associated SHP2/PTPN11 gene in human solid tumors and adult acute myelogenous leukemia". Cancer Res. 64 (24): 8816–20. doi:10.1158/0008-5472.CAN-04-1923. PMID 15604238.
  13. ^ Patel SS, Kuo FC, Gibson CJ, Steensma DP, Soiffer RJ, Alyea EP, Chen YA, Fathi AT, Graubert TA, Brunner AM, Wadleigh M, Stone RM, DeAngelo DJ, Nardi V, Hasserjian RP, Weinberg OK (May 2018). "High NPM1 mutant allele burden at diagnosis predicts unfavorable outcomes in de novo AML". Blood. 131 (25): 2816–2825. doi:10.1182/blood-2018-01-828467. PMC 6265642. PMID 29724895.
  14. ^ a b c Bard-Chapeau EA, Li S, Ding J, Zhang SS, Zhu HH, Princen F, Fang DD, Han T, Bailly-Maitre B, Poli V, Varki NM, Wang H, Feng GS (May 2011). "Ptpn11/Shp2 acts as a tumor suppressor in hepatocellular carcinogenesis". Cancer Cell. 19 (5): 629–39. doi:10.1016/j.ccr.2011.03.023. PMC 3098128. PMID 21575863.
  15. ^ a b Hatakeyama M, Higashi H (2005). "Helicobacter pylori CagA: a new paradigm for bacterial carcinogenesis". Cancer Science. 96 (12): 835–843. doi:10.1111/j.1349-7006.2005.00130.x. PMC 11159386. PMID 16367902. S2CID 5721063.
  16. ^ Tanaka Y, Tanaka N, Saeki Y, Tanaka K, Murakami M, Hirano T, Ishii N, Sugamura K (August 2008). "c-Cbl-dependent monoubiquitination and lysosomal degradation of gp130". Mol. Cell. Biol. 28 (15): 4805–18. doi:10.1128/MCB.01784-07. PMC 2493370. PMID 18519587.
  17. ^ Tauchi T, Feng GS, Marshall MS, Shen R, Mantel C, Pawson T, Broxmeyer HE (October 1994). "The ubiquitously expressed Syp phosphatase interacts with c-kit and Grb2 in hematopoietic cells". J. Biol. Chem. 269 (40): 25206–11. doi:10.1016/S0021-9258(17)31518-1. PMID 7523381.
  18. ^ Kozlowski M, Larose L, Lee F, Le DM, Rottapel R, Siminovitch KA (April 1998). "SHP-1 binds and negatively modulates the c-Kit receptor by interaction with tyrosine 569 in the c-Kit juxtamembrane domain". Mol. Cell. Biol. 18 (4): 2089–99. doi:10.1128/MCB.18.4.2089. PMC 121439. PMID 9528781.
  19. ^ Ilan N, Cheung L, Pinter E, Madri JA (July 2000). "Platelet-endothelial cell adhesion molecule-1 (CD31), a scaffolding molecule for selected catenin family members whose binding is mediated by different tyrosine and serine/threonine phosphorylation". J. Biol. Chem. 275 (28): 21435–43. doi:10.1074/jbc.M001857200. PMID 10801826.
  20. ^ Pumphrey NJ, Taylor V, Freeman S, Douglas MR, Bradfield PF, Young SP, Lord JM, Wakelam MJ, Bird IN, Salmon M, Buckley CD (April 1999). "Differential association of cytoplasmic signalling molecules SHP-1, SHP-2, SHIP and phospholipase C-gamma1 with PECAM-1/CD31". FEBS Lett. 450 (1–2): 77–83. doi:10.1016/S0014-5793(99)00446-9. PMID 10350061. S2CID 31471121.
  21. ^ Hua CT, Gamble JR, Vadas MA, Jackson DE (October 1998). "Recruitment and activation of SHP-1 protein-tyrosine phosphatase by human platelet endothelial cell adhesion molecule-1 (PECAM-1). Identification of immunoreceptor tyrosine-based inhibitory motif-like binding motifs and substrates". J. Biol. Chem. 273 (43): 28332–40. doi:10.1074/jbc.273.43.28332. PMID 9774457.
  22. ^ Jackson DE, Ward CM, Wang R, Newman PJ (March 1997). "The protein-tyrosine phosphatase SHP-2 binds platelet/endothelial cell adhesion molecule-1 (PECAM-1) and forms a distinct signaling complex during platelet aggregation. Evidence for a mechanistic link between PECAM-1- and integrin-mediated cellular signaling". J. Biol. Chem. 272 (11): 6986–93. doi:10.1074/jbc.272.11.6986. PMID 9054388.
  23. ^ Huber M, Izzi L, Grondin P, Houde C, Kunath T, Veillette A, Beauchemin N (January 1999). "The carboxyl-terminal region of biliary glycoprotein controls its tyrosine phosphorylation and association with protein-tyrosine phosphatases SHP-1 and SHP-2 in epithelial cells". J. Biol. Chem. 274 (1): 335–44. doi:10.1074/jbc.274.1.335. PMID 9867848.
  24. ^ Schulze WX, Deng L, Mann M (2005). "Phosphotyrosine interactome of the ErbB-receptor kinase family". Mol. Syst. Biol. 1 (1): E1–E13. doi:10.1038/msb4100012. PMC 1681463. PMID 16729043.
  25. ^ Tomic S, Greiser U, Lammers R, Kharitonenkov A, Imyanitov E, Ullrich A, Böhmer FD (September 1995). "Association of SH2 domain protein tyrosine phosphatases with the epidermal growth factor receptor in human tumor cells. Phosphatidic acid activates receptor dephosphorylation by PTP1C". J. Biol. Chem. 270 (36): 21277–84. doi:10.1074/jbc.270.36.21277. PMID 7673163.
  26. ^ a b c L.A. Lai, C. Zhao, E.E. Zhang, G.S. Feng (2004). "14 The Shp-2 tyrosine phosphatase". In Joaquín Ariño, Denis Alexander (eds.). Protein phosphatases. Springer. pp. 275–299. ISBN 978-3-540-20560-9.
  27. ^ a b Neel BG, Gu H, Pao L (June 2003). "The 'Shp'ing news: SH2 domain-containing tyrosine phosphatases in cell signaling". Trends in Biochemical Sciences. 28 (6): 284–293. doi:10.1016/S0968-0004(03)00091-4. ISSN 0968-0004. PMID 12826400.
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Further reading

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