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Article

Mutation of Ser-50 and Cys-66 in Snapin modulates protein structure and stability.

Biochemistry - 24 Apr 2012

Navarro Aaron, Encinar José A, López-Méndez Blanca, Aguado-Llera David, Prieto Jesús, Gómez Javier, Martínez-Cruz Luís Alfonso, Millet Oscar, González-Ros José Manuel, Fernández-Ballester Gregorio, Neira José L, Ferrer-Montiel Antonio

Abstract excerpt

Snapin is a 15 kDa protein present in neuronal and non-neuronal cells that has been implicated in the regulation of exocytosis and endocytosis. Protein kinase A (PKA) phosphorylates Snapin at Ser-50, modulating its function. Likewise, mutation of Cys-66, which mediates protein dimerization, impairs its cellular activity. Here, we have investigated the impact of mutating these two positions on protein...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Identifiers

PMID: 22471585
DOI: 10.1021/bi201574t

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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