Lymphocyte activation the coming of the protein tyrosine phosphatases

Mustelin, Tomas; Brockdorff, Johannes; Gjörloff-Wingren, Anette; Tailor, Pankaj; Han, Sun‐Young; Wang, X; Saxena, Manju

doi:10.2741/a346

Cited by 38 publications

(25 citation statements)

References 411 publications

(237 reference statements)

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“…First, as has been proposed by Tartaglia et al [2001Tartaglia et al [ , 2002, it is likely that the mutant SHP2 assumes a structure that is similar to the active state. Thus the opening of the SH2 PTPase interface may allow the PTPase constitutive access to its downstream substrates [Mustelin et al, 1998;Van Obberghen et al, 2001]. Alternatively, these missense mutations may alter the protein interactions of SHP2 such that it may fail to interact with one or more of its usual partners or fail to participate in specialized protein complexes [Okumura and Thomas, 1995;Ulyanova et al, 1997;Marron et al, 2000].…”

Section: Discussionmentioning

confidence: 99%

PTPN11 Mutations in Noonan syndrome type I: detection of recurrent mutations in exons 3 and 13

et al. 2002

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We surveyed 16 subjects with the clinical diagnosis of Noonan Syndrome (NS1) from 12 families and their relevant family members for mutations in PTPN11/SHP2 using direct DNA sequencing. We found three different mutations among five families. Two unrelated subjects shared the same de novo missense substitution in exon 13 (S502T); an additional two unrelated families had a mutation in exon 3 (Y63C); and one subject had the amino acid substitution Y62D, also in exon 3. None of the three mutations were present in ethnically matched controls. In the mature protein model, the exon 3 mutants and the exon 13 mutant amino acids cluster at the interface between the N' SH2 domain and the phosphatase catalytic domain. Six of eight subjects with PTPN11/SHP2 mutations had pulmonary valve stenosis while no mutations were identified in those subjects (N = 4) with hypertrophic cardiomyopathy. An additional four subjects with possible Noonan syndrome were evaluated, but no mutations in PTPN11/SHP2 were identified. These results confirm that mutations in PTPN11/SHP2 underlie a common form of Noonan syndrome, and that the disease exhibits both allelic and locus heterogeneity. The observation of recurrent mutations supports the hypothesis that a special class of gain-of-function mutations in SHP2 give rise to Noonan syndrome.

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Section: Discussionmentioning

confidence: 99%

PTPN11 Mutations in Noonan syndrome type I: detection of recurrent mutations in exons 3 and 13

et al. 2002

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“…PKA also induces activation of several genes that may contribute to immunosuppression and other physiological effects of cAMP 11 . Disturbances in the cAMP/PKA system have been implicated in human diseases such as lupus erythematosus 12 and immunosuppression associated with HIV infection 13 .Lymphocyte activation is also negatively regulated by several protein tyrosine phosphatases (PTPases), which counteract the protein tyrosine kinases (PTKs) involved in transmitting signals from occupied antigen receptors 14,15 . PTPases are structurally diverse enzymes, which share a conserved catalytic domain but differ markedly in their non-catalytic amino or carboxy termini 14,15 .…”

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confidence: 99%

Crosstalk between cAMP-dependent kinase and MAP kinase through a protein tyrosine phosphatase

et al. 1999

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The haematopoietic protein tyrosine phosphatase (HePTP) is a negative regulator of the MAP kinases Erk1, Erk2 and p38. HePTP binds to these kinases through a kinase-interaction motif (KIM) in its non-catalytic amino terminus and inactivates them by dephosphorylating the critical phosphorylated tyrosine residue in their activation loop. Here we show that cyclic-AMP-dependent protein kinase (PKA) phosphorylates serine residue 23 in the KIM of HePTP in vitro and in intact cells. This modification reduces binding of MAP kinases to the KIM, an effect that is prevented by mutation of serine 23 to alanine. The PKA-mediated release of MAP kinase from HePTP is sufficient to activate the kinase and to induce transcription from the c-fos promoter. Expression of a HePTP serine-23-to-alanine mutant inhibits MAP-kinase dissociation and activation and induction of transcription from the c-fos promoter. We conclude that HePTP not only controls the activity of MAP kinases, but also mediates crosstalk between the cAMP system and the MAP-kinase cascade.

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“…Therefore, recently cloned dual-speci¢city protein tyrosine phosphatase which exhibit dualcatalytic activity toward phosphotyrosine and phosphothreonine in substrate proteins, may play a crucial role in the regulation of MAPK signaling pathways (Bokemeyer et al, 1998). Ten di¡erent isoforms of MAPK phosphatases (MKP) have been discovered (Mustelin et al, 1998). MKP-1 has been identi¢ed as an immediate early gene.…”

Section: Introductionmentioning

confidence: 99%

Positive regulation of ERK activation and MKP-1 expression by peroxovanadium complex bpV (phen)

et al. 2004

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Lower micromolar concentrations of peroxovanadium compound potassium bisperoxo(1,10-phenanthroline)oxovanadate (V) [bpV (phen)] stimulate RINm5F cell metabolic activity. 1 and 3 micromol/L bpV (phen) induces strong and sustained activation of extracellular signal-regulated kinase (ERK). However, it seems that bpV (phen) does not effect c-Jun N-terminal kinase (JNK) and p38 mitogen-activated protein kinase (MAPK) phosphorylation. In addition, bpV (phen) induces mitogen-activated protein kinase phosphatase-1 (MKP-1) expression. We found that ERK activation could be completely abolished if RINm5F cells were incubated with both bpV (phen) and PD 98059, a specific inhibitor of upstream ERK kinase MEK1. On the other hand, this combined treatment up-regulated activation of stress kinases, JNK and p38 MAPK, significantly suppressed MKP-1 expression and induced cell death. Thus, our results suggest that the mechanism underlying bpV (phen) survival-enhancing effect could be associated with induced ERK activation and MKP-1 expression.

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Lymphocyte activation the coming of the protein tyrosine phosphatases

Cited by 38 publications

References 411 publications

PTPN11 Mutations in Noonan syndrome type I: detection of recurrent mutations in exons 3 and 13

PTPN11 Mutations in Noonan syndrome type I: detection of recurrent mutations in exons 3 and 13

Crosstalk between cAMP-dependent kinase and MAP kinase through a protein tyrosine phosphatase

Positive regulation of ERK activation and MKP-1 expression by peroxovanadium complex bpV (phen)

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