ArticleMolecular and cellular biochemistry2012
A calcium-dependent interaction between calmodulin and the calponin homology domain of human IQGAP1.
Article in Molecular and cellular biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Pleiotropic Roles of Calmodulin in the Regulation of KRas and Rac1 GTPases: Functional Diversity in Health and Disease.International journal of molecular sciences · 2020Review
- CaBiochemistry · 2019Article
- Over-expression of IQGAP1 indicates poor prognosis in head and neck squamous cell carcinoma.Journal of molecular histology · 2018Article
- The Calcium-Dependent Switch Helix of L-Plastin Regulates Actin Bundling.Scientific reports · 2017Article
- Article
- IQGAP1 is associated with nuclear envelope reformation and completion of abscission.Cell cycle (Georgetown, Tex.) · 2015Article
- A novel role for IQGAP1 protein in cell motility through cell retraction.Biochemical and biophysical research communications · 2014Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
IQGAPs are cytoskeletal scaffolding proteins which collect information from a variety of signalling pathways and pass it on to the microfilaments and microtubules. There is a well-characterised interaction between IQGAP and calmodulin through a series of IQ-motifs towards the middle of the primary sequence. However, it has been shown previously that the calponin homology domain (CHD), located at the N-terminus of the protein, can also interact weakly with calmodulin. Using a recombinant fragment of human IQGAP1 which encompasses the CHD, we have demonstrated that the CHD undergoes a calcium ion-dependent interaction with calmodulin. The CHD can also displace the hydrophobic fluorescent probe 1-anilinonaphthalene-8-sulphonate from calcium-calmodulin, suggesting that the interaction involves non-polar residues on the surface of calmodulin. Molecular modelling identified a possible site on the CHD for calmodulin interaction. The physiological significance of this interaction remains to be discovered.
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Registered trials
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