ArticleThe Journal of biological chemistry2012
Distinctive features of catalytic and transport mechanisms in mammalian sarco-endoplasmic reticulum Ca2+ ATPase (SERCA) and Cu+ (ATP7A/B) ATPases.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 38 citations in OpenAlex.
- Transmembrane Cu(I) P-type ATPase pumps are electrogenic uniporters.Dalton transactions (Cambridge, England : 2003) · 2020Article
- Protein Adsorption on Solid Supported Membranes: Monitoring the Transport Activity of P-Type ATPases.Molecules (Basel, Switzerland) · 2020Review
- Linking Biochemical and Structural States of SERCA: Achievements, Challenges, and New Opportunities.International journal of molecular sciences · 2020Review
- A case of a mild Wolfram Syndrome with concomitantCellR4-- repair, replacement, regeneration, & reprogramming · 2019Article
- Enhanced cellulase production by decreasing intercellular pH through HBiotechnology for biofuels · 2019Article
- Modulating Chemosensitivity of Tumors to Platinum-Based Antitumor Drugs by Transcriptional Regulation of Copper Homeostasis.International journal of molecular sciences · 2018Review
- Drug Interactions With the CaFrontiers in molecular biosciences · 2018Review
- Preexisting domain motions underlie protonation-dependent structural transitions of the P-type CaPhysical chemistry chemical physics : PCCP · 2017Article
- Characterization of ATP7A missense mutants suggests a correlation between intracellular trafficking and severity of Menkes disease.Scientific reports · 2017Article
- Hofmeister effect of anions on calcium translocation by sarcoplasmic reticulum Ca(2+)-ATPase.Scientific reports · 2015Article
- A sulfur-based transport pathway in Cu+-ATPases.EMBO reports · 2015Article
- Atomic-level mechanisms for phospholamban regulation of the calcium pump.Biophysical journal · 2015Article
- Biochemical characterization of P-type copper ATPases.The Biochemical journal · 2014Review
- Ca(2+)/H (+) exchange, lumenal Ca(2+) release and Ca (2+)/ATP coupling ratios in the sarcoplasmic reticulum ATPase.Journal of cell communication and signaling · 2014Article
- Translocation of platinum anticancer drugs by human copper ATPases ATP7A and ATP7B.Angewandte Chemie (International ed. in English) · 2014Article
- Copper-transporting P-type ATPases use a unique ion-release pathway.Nature structural & molecular biology · 2014Article
- Golgi in copper homeostasis: a view from the membrane trafficking field.Histochemistry and cell biology · 2013Review
- Istaroxime stimulates SERCA2a and accelerates calcium cycling in heart failure by relieving phospholamban inhibition.British journal of pharmacology · 2013Article
- Ion pathways in the sarcoplasmic reticulum Ca2+-ATPase.The Journal of biological chemistry · 2013Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Ca(2+) (sarco-endoplasmic reticulum Ca(2+) ATPase (SERCA)) and Cu(+) (ATP7A/B) ATPases utilize ATP through formation of a phosphoenzyme intermediate (E-P) whereby phosphorylation potential affects affinity and orientation of bound cation. SERCA E-P formation is rate-limited by enzyme activation by Ca(2+), demonstrated by the addition of ATP and Ca(2+) to SERCA deprived of Ca(2+) (E2) as compared with ATP to Ca(2+)-activated enzyme (E1·2Ca(2+)). Activation by Ca(2+) is slower at low pH (2H(+)·E2 to E1·2Ca(2+)) and little sensitive to temperature-dependent activation energy. On the other hand, subsequent (forward or reverse) phosphoenzyme processing is sensitive to activation energy, which relieves conformational constraints limiting Ca(2+) translocation. A "H(+)-gated pathway," demonstrated by experiments on pH variations, charge transfer, and Glu-309 mutation allows luminal Ca(2+) release by H(+)/Ca(2+) exchange. As compared with SERCA, initial utilization of ATP by ATP7A/B is much slower and highly sensitive to temperature-dependent activation energy, suggesting conformational constraints of the headpiece domains. Contrary to SERCA, ATP7B phosphoenzyme cleavage shows much lower temperature dependence than EP formation. ATP-dependent charge transfer in ATP7A and -B is observed, with no variation of net charge upon pH changes and no evidence of Cu(+)/H(+) exchange. As opposed to SERCA after Ca(2+) chelation, ATP7A/B does not undergo reverse phosphorylation with P(i) after copper chelation unless a large N-metal binding extension segment is deleted. This is attributed to the inactivating interaction of the copper-deprived N-metal binding extension with the headpiece domains. We conclude that in addition to common (P-type) phosphoenzyme intermediate formation, SERCA and ATP7A/B possess distinctive features of catalytic and transport mechanisms.
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