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Article

Identification of novel anionic phospholipid binding domains in neutral sphingomyelinase 2 with selective binding preference.

The Journal of biological chemistry - 24 Jun 2011

Wu Bill X, Clarke Christopher J, Matmati Nabil, Montefusco David, Bartke Nana, Hannun Yusuf A

Abstract excerpt

Sphingolipids such as ceramide are recognized as vital regulators of many biological processes. Neutral sphingomyelinase 2 (nSMase2) is one of the key enzymes regulating ceramide production. It was previously shown that the enzymatic activity of nSMase2 was dependent on anionic phospholipids (APLs). In this study, the structural requirements for APL-selective binding of nSMase2 were determined and characterized....

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Identifiers

PMID: 21550973
DOI: 10.1074/jbc.M110.156471
PMCID: PMC3121384

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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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