Mechanism of Ser88 phosphorylation-induced dimer dissociation in dynein light chain LC8.

doi:10.1021/jp1048869

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Back to search

Article

Mechanism of Ser88 phosphorylation-induced dimer dissociation in dynein light chain LC8.

The journal of physical chemistry. B - 2 Dec 2010

Xiao Fei, Weng Jingwei, Fan Kangnian, Wang Wenning

Abstract excerpt

Dynein light chain LC8 is a highly conserved, dimeric protein involved in a variety of essential cellular events. Phosphorylation at Ser88 was found to promote mammalian cell survival and regulate the dimer to monomer transition at physiological pH. Combining molecular dynamics (MD) simulation and free energy calculation methods, we explored the atomistic mechanism of the phosphorylation-induced dimer...

Topics

Cytoplasmic Dyneins
Dimerization
Hydrogen Bonding
Hydrogen-Ion Concentration
Molecular Dynamics Simulation
Mutation
Phosphorylation
Plant Proteins
Protein Structure, Tertiary
Serine
Thermodynamics

Source

Open in PubMed

Identifiers

PMID: 21062069
DOI: 10.1021/jp1048869

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics