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LCTS built a strong track record in the research area of the P2-type ATPases, the primary cellular Ca2+ transporters. More specifically, the lab contributed to important discoveries on the structure-function relationship and physiological role of the sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA) pumps and the secretory pathway Ca2+- ATPase (SPCA) isoforms.


Highlights of our work

An N-terminal Ca2+-binding motif regulates the secretory pathway Ca2+/Mn2+-transport ATPase SPCA1

During her work as a Ph.D. student, Jialin established a new recombinant purification protocol and a reconstitution system in proteoliposomes which enabled her to study the biochemical properties of SPCA1a and SPCA2. She revealed important differences in the regulatory mechanism and enzyme kinetics between the two isoforms. These findings may be of physiological relevance in cell types where SPCA function is critical such as the mammary gland or keratinocytes. Interestingly, mutations in SPCA have been associated with breast cancer and Hailey-Hailey skin disease.

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MAY 2019, JBC

In close collaboration between our lab and the group of Poul Nissen at the Aarhus University in Denmark, Dr. Alya revealed the first crystal structures of SERCA2a, determined in CPA-stabilized E2-AlF4 form (3.3 Å) and the Ca2+-occluded [Ca2]E1-AMPPCP form (4.0 Å). Additionally, Alya and her colleagues identified key isoform-specific residues (SERCA2a versus SERCA1a) that are important acceptor sites for post-translational modifications and may contribute to the kinetic differences between the two isoforms.

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Structures of the heart specific SERCA2a Ca2+-ATPase

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