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C-mip interacts with the p85 subunit of PI3 kinase and exerts a dual effect on ERK signaling via the recruitment of Dip1 and DAP kinase |
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| Authors: | Maud Kamal Andre Pawlak Fatima BenMohamed Asta Valanciuté Karine Dahan Marina Candelier Philippe Lang Georges Guellaën Djillali Sahali |
| Institution: | a INSERM, U 955, Equipe 21, Créteil F-94010, France b Université Paris 12, Faculté de Médecine, UMRS 955, Equipe 21, Créteil, F-94010, France c AP-HP, Groupe hospitalier Henri Mondor - Albert Chenevier, Service de Néphrologie, Créteil F-94010, France d Institut Francilien de Recheche en Nephrologie et Transplantation, Hopital Henri Mondor, France |
| Abstract: | In naive T cells, Lck exerts a negative control on the ERK/MAPK pathway. We show that c-mip (c-maf inducing protein) interacts with the p85 subunit of PI3 kinase and inactivates Lck, which results in Erk1/2 and p38 MAPK activation. This effect is not enough to activate AP1 given the inability of ERK to migrate into the nucleus and to transactivate its target genes. We demonstrate that c-mip interacts with Dip1 and upregulates DAPK, which blocks the nuclear translocation of ERK1/2. This dual effect of c-mip is unique and might represent a potential mechanism to prevent the development of an immune response.Structured summaryMINT-7383650: p85 (uniprotkb:P27986) physically interacts (MI:0915) with c-Mip (uniprotkb:Q8IY22) by anti bait coimmunoprecipitation (MI:0006)MINT-7383661: c-Mip (uniprotkb:Q8IY22) physically interacts (MI:0915) with p85 (uniprotkb:P27986) by anti tag coimmunoprecipitation (MI:0007)MINT-7383676: p85 (uniprotkb:P27986) physically interacts (MI:0915) with p110 (uniprotkb:P42336) by anti bait coimmunoprecipitation (MI:0006)MINT-7383689, MINT-7383711: Dip-1 (uniprotkb:Q80SY4) physically interacts (MI:0915) with c-Mip (uniprotkb:Q8IY22) by anti tag coimmunoprecipitation (MI:0007) |
| Keywords: | C-mip PI3 kinase Lck DIP1 DAP-kinase ERK signaling |
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