ArticleProtein science : a publication of the Protein Society2005
Calcium- and magnesium-dependent interactions between calcium- and integrin-binding protein and the integrin alphaIIb cytoplasmic domain.
Article in Protein science : a publication of the Protein Society, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 47 citations in OpenAlex.
- The Diverse Functions of the Calcium- and Integrin-Binding Protein Family.International journal of molecular sciences · 2025Review
- High-throughput identification of calcium-regulated proteins across diverse proteomes.Cell reports · 2024Article
- High-Throughput Identification of Calcium Regulated Proteins Across Diverse Proteomes.bioRxiv : the preprint server for biology · 2024Article
- Discovery and Characterization of Peptide Inhibitors for Calcium and Integrin Binding Protein 1.ACS chemical biology · 2020Article
- Variants in CIB2 cause DFNB48 and not USH1J.Clinical genetics · 2018Article
- An nMgO containing scaffold: Antibacterial activity, degradation properties and cell responses.International journal of bioprinting · 2018Article
- Preferential Binding of MgFrontiers in molecular neuroscience · 2018Article
- CIB1: a small protein with big ambitions.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2016Review
- DFT and docking studies of rhodostreptomycins A and B and their interactions with solvated/nonsolvated Mg²⁺ and Ca²⁺ ions.Journal of molecular modeling · 2013Article
- Identification of novel integrin binding partners for calcium and integrin binding protein 1 (CIB1): structural and thermodynamic basis of CIB1 promiscuity.Biochemistry · 2013Article
- Structural basis for the activation of platelet integrin αIIbβ3 by calcium- and integrin-binding protein 1.Journal of the American Chemical Society · 2012Article
- Solution structures of Ca2+-CIB1 and Mg2+-CIB1 and their interactions with the platelet integrin alphaIIb cytoplasmic domain.The Journal of biological chemistry · 2011Article
- Structural analysis of Mg2+ and Ca2+ binding, myristoylation, and dimerization of the neuronal calcium sensor and visinin-like protein 1 (VILIP-1).The Journal of biological chemistry · 2011Article
- The solution structure of the Mg2+ form of soybean calmodulin isoform 4 reveals unique features of plant calmodulins in resting cells.Protein science : a publication of the Protein Society · 2010Article
- Translocation of sphingosine kinase 1 to the plasma membrane is mediated by calcium- and integrin-binding protein 1.The Journal of biological chemistry · 2010Article
- Effect of metal ion substitutions in anticoagulation factor I from the venom of Agkistrodon acutus on the binding of activated coagulation factor X and on structural stability.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2009Article
- Characterization of calcium- and integrin-binding protein 1 (CIB1) knockout platelets: potential compensation by CIB family members.Thrombosis and haemostasis · 2008Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Calcium- and integrin-binding protein (CIB) is a small EF-hand calcium-binding protein that is involved in hemostasis through its interaction with the alphaIIb cytoplasmic domain of integrinalphaIIbbeta(3). We have previously demonstrated that CIB lacks structural stability in the absence of divalent metal ions but that it acquires a well-folded conformation upon addition of Ca(2+) or Mg(2+). Here, we have used fluorescence spectroscopy, NMR spectroscopy, and isothermal titration calorimetry to demonstrate that both Ca(2+)-bound CIB (Ca(2+)-CIB) and the Mg(2+)-bound protein (Mg(2+)-CIB) bind with high affinity and through a similar mechanism to alphaIIb cytoplasmic domain peptides, but that metal-free CIB (apo-CIB) binds in a different manner. The interactions are thermodynamically distinct for Ca(2+)-CIB and Mg(2+)-CIB, but involve hydrophobic interactions in each case. Since the Mg(2+) concentration inside the cell is sufficient to saturate CIB at all times, our results imply that CIB would be capable of binding to the alphaIIb cytoplasmic domain independent of an intracellular Ca(2+) stimulus in vivo. This raises the question of whether CIB can act as a Ca(2+) sensor in alphaIIbbeta(3) signaling or if other regulatory mechanisms such as fibrinogen-induced conformational changes in alphaIIbbeta(3), post-translational modifications, or the binding of other accessory proteins mediate the interactions between CIB and alphaIIbbeta(3). Differences in NMR spectra do suggest, however, that Ca(2+)-binding to the Mg(2+)- CIB-alphaIIb complex induces subtle structural changes that could further modulate the activity of alphaIIbbeta(3).
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