ArticleMolecules and cells2011
Characterization of novel calmodulin binding domains within IQ motifs of IQGAP1.
Article in Molecules and cells, 2011. 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, 16 citations in OpenAlex.
- The co-occurrence of homozygous variants in GUCY2D and MYO7A in Leber congenital amaurosis associated with deafness: clinical, molecular, and in silico investigation.Molecular biology reports · 2026Article
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- IQGAP1 promotes chronic pain by regulating the trafficking and sensitization of TRPA1 channels.Brain : a journal of neurology · 2023Article
- Spatiotemporal restriction of endothelial cell calcium signaling is required during leukocyte transmigration.The Journal of experimental medicine · 2021Article
- The Role of Calmodulin in Tumor Cell Migration, Invasiveness, and Metastasis.International journal of molecular sciences · 2020Review
- Endothelial IQGAP1 regulates leukocyte transmigration by directing the LBRC to the site of diapedesis.The Journal of experimental medicine · 2019Article
- Development of LC3/GABARAP sensors containing a LIR and a hydrophobic domain to monitor autophagy.The EMBO journal · 2017Article
- UBE3B Is a Calmodulin-regulated, Mitochondrion-associated E3 Ubiquitin Ligase.The Journal of biological chemistry · 2017Article
- W342F Mutation in CCaMK Enhances Its Affinity to Calmodulin But Compromises Its Role in Supporting Root Nodule Symbiosis inFrontiers in plant science · 2017Article
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- Article
- Characterization of the cellular localization of C4orf34 as a novel endoplasmic reticulum resident protein.BMB reports · 2014Article
- A calcium-dependent interaction between calmodulin and the calponin homology domain of human IQGAP1.Molecular and cellular biochemistry · 2012Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
IQ motif-containing GTPase-activating protein 1 (IQGAP1), which is a well-known calmodulin (CaM) binding protein, is involved in a wide range of cellular processes including cell proliferation, tumorigenesis, adhesion, and migration. Interaction of IQGAP1 with CaM is important for its cellular functions. Although each IQ domain of IQGAP1 for CaM binding has been characterized in a Ca(2+)-dependent or -independent manner, it was not clear which IQ motifs are physiologically relevant for CaM binding in the cells. In this study, we performed immunoprecipitation using 3xFLAGhCaM in mammalian cell lines to characterize the domains of IQGAP1 that are key for CaM binding under physiological conditions. Interestingly, using this method, we identified two novel domains, IQ(2.7-3) and IQ(3.5-4.4), within IQGAP1 that were involved in Ca(2+)-independent or -dependent CaM binding, respectively. Mutant analysis clearly showed that the hydrophobic regions within IQ(2.7-3) were mainly involved in apoCaM binding, while the basic amino acids and hydrophobic region of IQ(3.5-4.4) were required for Ca(2+)/CaM binding. Finally, we showed that IQ(2.7-3) was the main apoCaM binding domain and both IQ(2.7-3) and IQ(3.5-4.4) were required for Ca(2+)/CaM binding within IQ(1-2-3-4). Thus, we identified and characterized novel direct CaM binding motifs essential for IQGAP1. This finding indicates that IQGAP1 plays a dynamic role via direct interactions with CaM in a Ca(2+)-dependent or -independent manner.
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