ArticleBMC structural biology2009
The Sam domain of the lipid phosphatase Ship2 adopts a common model to interact with Arap3-Sam and EphA2-Sam.
Article in BMC structural biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- The Interaction between the Tyrosine Kinase Receptor EphA2 and RNF5: Structural Insights from anComputational and structural biotechnology journal · 2026Article
- Exploring a Potential Optimization Route for Peptide Ligands of the Sam Domain from the Lipid Phosphatase Ship2.International journal of molecular sciences · 2024Article
- Sticky, Adaptable, and Many-sided: SAM protein versatility in normal and pathological hematopoietic states.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023Review
- Hunting for Novel Routes in Anticancer Drug Discovery: Peptides against Sam-Sam Interactions.International journal of molecular sciences · 2022Review
- Targeting SHIP1 and SHIP2 in Cancer.Cancers · 2021Review
- Aβ modulates actin cytoskeleton via SHIP2-mediated phosphoinositide metabolism.Scientific reports · 2019Article
- Specific Eph receptor-cytoplasmic effector signaling mediated by SAM-SAM domain interactions.eLife · 2018Article
- The Sam-Sam interaction between Ship2 and the EphA2 receptor: design and analysis of peptide inhibitors.Scientific reports · 2017Article
- Characterization of the SAM domain of the PKD-related protein ANKS6 and its interaction with ANKS3.BMC structural biology · 2014Article
- ARAP3 functions in hematopoietic stem cells.PloS one · 2014Article
- Heterotypic Sam-Sam association between Odin-Sam1 and Arap3-Sam: binding affinity and structural insights.Chembiochem : a European journal of chemical biology · 2013Article
- Biochemistry and structure of phosphoinositide phosphatases.BMB reports · 2013Review
- Solution structure of the first Sam domain of Odin and binding studies with the EphA2 receptor.Biochemistry · 2012Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
backgroundSterile alpha motif (Sam) domains are small protein modules that can be involved in homotypic or heterotypic associations and exhibit different functions. Previous studies have demonstrated that the Sam domain of the lipid phosphatase Ship2 can hetero-dimerize with the Sam domain of the PI3K effector protein Arap3.
resultsHere, we determine the NMR solution structure of Arap3-Sam and implement a multidisciplinary approach consisting of NMR spectroscopy, ITC (Isothermal Titration Calorimetry), mutagenesis and molecular modeling studies to analyze the interaction between Ship2-Sam and Arap3-Sam. This work reveals that Arap3-Sam may associate with Ship2-Sam by adopting a binding mode common to other Sam domains. This binding mode is identical to what we have very recently observed for the association between Ship2-Sam and the Sam domain from the Ephrin A2 receptor.
conclusionOur studies further clarify the structural features that are relevant for Sam-Sam interactions involving Ship2 and give additional hints that could be used for the identification of new molecules able to selectively inhibit Sam-Sam associations.
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