Lipid chain-driven interaction of a lipidated Src-family kinase Lyn with the bilayer membrane-Reference-Cited by-同舟云学术

Lipid chain-driven interaction of a lipidated Src-family kinase Lyn with the bilayer membrane

Published:2022 Issue:32 Volume:20 Page:6436-6444
ISSN:1477-0520
Container-title:Organic & Biomolecular Chemistry
language:en
Short-container-title:Org. Biomol. Chem.

Author:

Hanashima Shinya¹^ORCID,Mito Kanako¹,Umegawa Yuichi¹,Murata Michio¹²^ORCID,Hojo Hironobu²³^ORCID

Affiliation:

1. Department of Chemistry, Graduate School of Science, Osaka University, 1-1 Machikaneyama-cho, Toyonaka, Osaka 560-0043, Japan

2. Forefront Research Center, Graduate School of Science, Osaka University, Toyonaka, Osaka 560-0043, Japan

3. Institute for Protein Research, Osaka University, Yamadaoka 3-2, Suita 565-0871, Japan

Abstract

S-Palmitoyl and N-myristoyl chains of Lyn cooperatively facilitate binding to the anionic lipids in membranes by extending the hydrocarbon chains deeper into the membrane interior.

Funder

Japan Society for the Promotion of Science

Core Research for Evolutional Science and Technology

Publisher

Royal Society of Chemistry (RSC)

Subject

Organic Chemistry,Physical and Theoretical Chemistry,Biochemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2022/OB/D2OB01079H

Reference54 articles.

1. Protein Lipidation: Occurrence, Mechanisms, Biological Functions, and Enabling Technologies

2. Protein N-myristoylation: functions and mechanisms in control of innate immunity

3. Binding of acylated peptides and fatty acids to phospholipid vesicles: Pertinence to myristoylated proteins

4. Doubly-lipid-modified protein sequence motifs exhibit long-lived anchorage to lipid bilayer membranes

5. Fatty acylation of proteins: The long and the short of it

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