» Articles » PMID: 16624617

Phosphatidic Acid- and Phosphatidylserine-binding Proteins

Overview
Specialties Biochemistry
Biophysics
Date 2006 Apr 21
PMID 16624617
Citations 181
Authors
Affiliations
Soon will be listed here.
Abstract

Phosphatidic acid and phosphatidylserine are negatively charged abundant phospholipids with well-recognized structural roles in cellular membranes. They are also signaling lipids since their regulated formation (or appearance) can constitute an important signal for downstream responses. The list of potential effectors for these lipids is expanding rapidly and includes proteins involved in virtually all aspects of cellular regulation. Because it is not always clear whether these effectors recognize the specific phospholipids or a general negatively-charged membrane environment, questions about specificity must be addressed on a case by case basis. In this review we present an up to date list of potential phosphatidic acid- and phosphatidylserine-binding proteins.

Citing Articles

The Role of Protein-Lipid Interactions in Priming the Bacterial Translocon.

Sinclair M, Tajkhorshid E Membranes (Basel). 2024; 14(12).

PMID: 39728699 PMC: 11677795. DOI: 10.3390/membranes14120249.


Can calmodulin bind to lipids of the cytosolic leaflet of plasma membranes?.

Scollo F, Tempra C, Evci H, Riopedre-Fernandez M, Olzynska A, Javanainen M Open Biol. 2024; 14(9):240067.

PMID: 39288811 PMC: 11500697. DOI: 10.1098/rsob.240067.


Molecular insights into human phosphatidylserine synthase 1 reveal its inhibition promotes LDL uptake.

Long T, Li D, Vale G, Jiang Y, Schmiege P, Yang Z Cell. 2024; 187(20):5665-5678.e18.

PMID: 39208797 PMC: 11455612. DOI: 10.1016/j.cell.2024.08.004.


Efferocytosis and Bone Dynamics.

Batoon L, Hawse J, McCauley L, Weivoda M, Roca H Curr Osteoporos Rep. 2024; 22(5):471-482.

PMID: 38914730 DOI: 10.1007/s11914-024-00878-y.


Membrane binding and lipid-protein interaction of the C2 domain from coagulation factor V.

Ohkubo Y, Radulovic P, Kahira A, Madsen J Curr Res Struct Biol. 2024; 7:100149.

PMID: 38766652 PMC: 11098723. DOI: 10.1016/j.crstbi.2024.100149.