The SH2-domain of SHIP1 interacts with the SHIP1 C-terminus: Impact on SHIP1/Ig-α interaction
Open accessAbstract
The SH2-containing inositol 5'-phosphatase, SHIP1, negatively regulates signal transduction from the B cell antigen receptor (BCR). The mode of coupling between SHIP1 and the BCR has not been elucidated so far. In comparison to wild-type cells, B cells expressing a mutant IgD- or IgM-BCR containing a C-terminally truncated Ig-α respond to pervanadate stimulation with markedly reduced tyrosine phosphorylation of SHIP1 and augmented activation of protein kinase B. This indicates that SHIP1 is capable of interacting with the C-terminus of Ig-α. Employing a system of fluorescence resonance energy transfer in S2 cells, we can clearly demonstrate interaction between the SH2-domain of SHIP1 and Ig-α. Furthermore, a fluorescently labeled SH2-domain of SHIP1 translocates to the plasma membrane in an Ig-α-dependent manner. Interestingly, whereas the SHIP1 SH2-domain can be pulled-down with phospho-peptides corresponding to the immunoreceptor tyrosine-based activation motif (ITAM) of Ig-α from detergent lysates, no interaction between full-length SHIP1 and the phosphorylated Ig-α ITAM can be observed. Further studies show that the SH2-domain of SHIP1 can bind to the C-terminus of the SHIP1 molecule, most probably by inter- as well as intra-molecular means, and that this interaction regulates the association between different forms of SHIP1 and Ig-α.
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Phosphorylation of SHIP1 at Tyr1022 within the NPxY motif allows binding with SHIP1's own SH2 domain, which may mediate its dimerization or oligomerization.
“Phosphorylation of SHIP1 at Tyr1022 within the NPxY motif allows binding with SHIP1’s own SH2 domain, which may mediate its dimerization or oligomerization.”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [113]
Section 3.7 and Fig. 6 support binding of SHIP1’s SH2 domain to a phosphorylated NPxY-region peptide and examine SHIP1 dimerization or oligomerization. The Discussion describes possible inter- and intramolecular interactions. However, the paper consistently identifies the tyrosine as Y1020, not Tyr1022. (LLM, conf=0.88)
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- Authors
- Mukherjee, O., Weingarten, L., Padberg, I., Pracht, C., Sinha, R., Hochdörfer, T., Kuppig, S., Backofen, R., Reth, M., & Huber, M.
- Affiliations
- RWTH Aachen University (DE)
- Max Planck Society (DE)
- University of Freiburg (DE)
- Corresponding author
- Huber, Michael
- ORCID
- Venue
- Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
- Publisher
- Elsevier BV
- Published
- 2012-02
- Volume
- 1823
- Issue
- 2
- Pages
- 206-214
- ISSN
- 0167-4889 (ISSN-L)
- OpenAlex
- W2024496465
- Cited by
- 20
- References
- 60
- Citations by year
- 2026: 4 · 2025: 2 · 2024: 1 · 2023: 4 · 2022: 2 · 2020: 1 · 2017: 1 · 2016: 2 · 2013: 1 · 2012: 2
- FWCI
- 0.42
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Biochimica et Biophysica Acta (BBA) - Molecular Cell Research (publishedVersion)
- PubMed (publishedVersion)
- Max Planck Digital Library (submittedVersion)
- RWTH Publications (RWTH Aachen) (submittedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion)
- Funders
- Deutsche Forschungsgemeinschaft (Hu794/3-2, Hu794/8-1)
- Excellence Initiative of the German Federal and State Governments (EXC 294)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › T-cell and B-cell Immunology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- SHIP1, SH2 domain, Ig-alpha, B cell receptor, inositol polyphosphate 5-phosphatase, ITAM, tyrosine phosphorylation, Akt, pervanadate, plasma membrane translocation, B cell signaling
- MeSH terms
- Inositol Polyphosphate 5-Phosphatases, Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases, Animals, B-Lymphocytes, Cell Membrane, Immunoglobulin alpha-Chains, Phosphoric Monoester Hydrolases, Recombinant Fusion Proteins, Tumor Cells, Cultured, src Homology Domains, Dimerization, Mice
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