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Article

An important functional role of the N terminus domain of type VI adenylyl cyclase in Galphai-mediated inhibition.

The Journal of biological chemistry - 13 Aug 2004

Kao Yu-Ya, Lai Hsing-Lin, Hwang Ming-Jing, Chern Yijuang

Abstract excerpt

We show herein that removal of the first 86 amino acids (aa) of the N terminus (designated N) of type VI adenylyl cyclase (ACVI) caused the resultant ACVI mutant (ACVI-DeltaA87) to be more greatly inhibited by a Galpha(i)-coupled receptor or activated Galpha(i) protein. Moreover, in vitro binding of the full-length N and C1a domain (designated C1a), which interacts with Galpha(i), was detected. A truncated N...

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PMID: 15192109
DOI: 10.1074/jbc.M401952200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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