Structural Basis for Diversity of the EF-hand Calcium-binding Proteins

Grabarek, Zenon

doi:10.1016/j.jmb.2006.03.066

Cited by 343 publications

(380 citation statements)

References 147 publications

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“…It may also play a role in regulating the kinetics of signaling in the phototransduction cascade. The calcium-binding proteins of the EF-hand super family are involved in the regulation of all aspects of cell function (Grabarek, 2006). The ZWINT encoded-protein plays a critical role in cell mitosis and will be changed with cell cycle (Obuse et al, 2004).…”

Section: Discussionmentioning

confidence: 99%

A Genome-Wide Scan of DNA Methylation Markers for Distinguishing Monozygotic Twins

Zhu

et al. 2015

Twin Res Hum Genet

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Identification of individuals within pairs of monozygotic (MZ) twins remains unresolved using common forensic DNA typing technology. For some criminal cases involving MZ twins as suspects, the twins had to be released due to inability to identify which of the pair was the perpetrator. In this study, we performed a genome-wide scan on whole blood-derived DNA from four pairs of healthy phenotypically concordant MZ twins using the methylated DNA immunoprecipitation sequencing technology to identify candidate DNA methylation markers with capacity to distinguish MZ twins within a pair. We identified 38 differential methylation regions showing within-pair methylation differences in all four MZ pairs. These are all located in CpG islands, 17 of which are promoter-associated, 17 are intergenic islands, and four are intragenic islands. Genes associated with these markers are related with cell proliferation, differentiation, and growth and development, including zinc finger proteins, PRRX2, RBBP9, or are involved in G-protein signaling, such as the regulator of G-protein signaling 16. Further validation studies on additional MZ twins are now required to evaluate the broader utility of these 38 markers for forensic use.

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Section: Discussionmentioning

confidence: 99%

A Genome-Wide Scan of DNA Methylation Markers for Distinguishing Monozygotic Twins

Zhu

et al. 2015

Twin Res Hum Genet

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“…This 13-residue loop is conserved in all known vertebrate PLCη enzymes (including mammals, amphibians, birds and fish; Figure S1), suggesting that this motif is (or was) functionally important and originated (probably due to a codon insertion event) prior to the divergence of vertebrates 500 million years ago. Non-canonical loops have been identified in a number of EF-hand-containing proteins, which in some cases are able to coordinate to Ca 2+ (Gifford et al, 2007;Grabarek, 2006). An example (human calbindin D 9K ) is illustrated in the alignment in Figure 1D.…”

Section: Analysis Of Ef-hand Domains From Plcη Enzymesmentioning

confidence: 99%

“…Within the EF-hand these two motifs are stacked against one another in a face-to-face manner. This structure is further stabilized by a short antiparallel β-sheet formed between the pairs' EF-loops (Grabarek, 2006). The structural and metal ion-binding properties of these domains are reviewed by Gifford et al (2007).…”

Section: Introductionmentioning

confidence: 99%

A Canonical EF‐Loop Directs Ca²⁺‐Sensitivity in Phospholipase C‐η2

Popovics

Kamil

Morgan

et al. 2014

J of Cellular Biochemistry

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Phospholipase C-ɳ(PLCɳ) enzymes are a class of phosphatidylinositol 4,5-bisphosphatehydrolyzing enzymes involved in intracellular signaling. PLCɳ2 can sense Ca 2+ (stimulated bỹ 1 µM free Ca 2+ ) suggesting that it can amplify transient Ca 2+ signals. PLCɳ enzymes possess an EF-hand domain composed of two EF-loops; a canonical 12-residue loop (EF-loop 1) and a non-canonical 13-residue loop (EF-loop 2). Ca 2+ -binding to synthetic peptides corresponding to EF-loops 1 and 2 of PLCɳ2 and EF-loop 1 of calmodulin (as a control) was examined by 2D-[ 1 H, 1 H] TOCSY NMR. Both PLCɳ2 EF-loop peptides bound Ca 2+ in a similar manner to that of the canonical calmodulin EF-loop 1, particularly at their N-terminus. A molecular model of the PLCɳ2 EF-hand domain, constructed based upon the structure of calmodulin, suggested both EF-loops may participate in Ca 2+ -binding. To determine whether the EF-hand is responsible for Ca 2+ -sensing, inositol phosphate accumulation was measured in COS7 cells transiently expressing wild-type or mutant PLCɳ2 proteins. Addition of 70µM monensin (a Na + /H + antiporter that increases intracellular Ca 2+ ) induced a 4 to 7-fold increase in wild-type PLCɳ2 activity. In permeabilized cells, PLCn2 exhibited a ~4-fold increase in activity in the presence of 1 µM free Ca 2+ . The D256A (EF-loop1) mutant exhibited a ~10-fold reduction in Ca 2+ -sensitivity and was not activated by monensin, highlighting the involvement of EF-loop 1 in Ca 2+ -sensing. Involvement of EF-loop 2 was examined using D292A, H296A, Q297A and E304A mutants. Interestingly, the monensin responses and Ca 2+ -sensitivities were largely unaffected by the mutations, indicating that the non-canonical EF-loop 2 is not involved in Ca 2+ -sensing.

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“…CaM has four high-affinity calcium binding sites called EF-hands, each composed of two ␣-helices connected by a calcium binding loop (reviewed in ref. 13). Calcium binding to CaM triggers a major change in the orientation of the helices that results in the so-called ''open'' conformation for both lobes of CaM (10,11,14).…”

mentioning

confidence: 99%

Crystal structure of apo-calmodulin bound to the first two IQ motifs of myosin V reveals essential recognition features

Houdusse

Gaucher

Krementsova

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

130

216

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Structural Basis for Diversity of the EF-hand Calcium-binding Proteins

Cited by 343 publications

References 147 publications

A Genome-Wide Scan of DNA Methylation Markers for Distinguishing Monozygotic Twins

A Genome-Wide Scan of DNA Methylation Markers for Distinguishing Monozygotic Twins

A Canonical EF‐Loop Directs Ca²⁺‐Sensitivity in Phospholipase C‐η2

Crystal structure of apo-calmodulin bound to the first two IQ motifs of myosin V reveals essential recognition features

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Structural Basis for Diversity of the EF-hand Calcium-binding Proteins

Cited by 343 publications

References 147 publications

A Genome-Wide Scan of DNA Methylation Markers for Distinguishing Monozygotic Twins

A Genome-Wide Scan of DNA Methylation Markers for Distinguishing Monozygotic Twins

A Canonical EF‐Loop Directs Ca2+‐Sensitivity in Phospholipase C‐η2

Crystal structure of apo-calmodulin bound to the first two IQ motifs of myosin V reveals essential recognition features

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A Canonical EF‐Loop Directs Ca²⁺‐Sensitivity in Phospholipase C‐η2