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Structural basis of activation and inhibition of the Ca2+/calmodulin-sensitive adenylyl cyclase 8 (XL-MS)

ABSTRACT: Membrane adenylyl cyclases (ACs) catalyze the conversion of ATP to cAMP, a second messenger involved in different signaling pathways. AC8 is one of the 9 membrane-bound isoforms, present in the brain and implicated in cognitive functions. AC8 is regulated by Ca2+/CaM and different G proteins but structural evidence on its regulation is scarce. We solved the structure of full-length AC8 in complex with Gas and CaM. ACs contain large stretches of disordered/highly flexible domains that cannot be resolved with cryo-EM. To overcome this limitation, we have studied AC8's interaction with CaM, Gas and Gbg using crosslinking mass spectrometry (XL-MS).

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Bos Taurus (bovine)

SUBMITTER: Dina Schuster

LAB HEAD: Volodymyr M. Korkhov

PROVIDER: PXD040374 | Pride | 2024-02-14

REPOSITORIES: Pride

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			Action	DRS
	211111_LU02_dschuster_P04_697.raw	Raw
	211111_LU02_dschuster_P04_697_2.raw	Raw
	211111_LU02_dschuster_P04_698.raw	Raw
	211111_LU02_dschuster_P04_698_2.raw	Raw
	211111_LU02_dschuster_P04_699.raw	Raw

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