Phospholipid distribution around the plasma membrane calcium pump: a hydrophobic photolabeling study.

Abstract:

:The functions of membrane proteins are highly dependent on their phospholipid environment. In this article, we have used a hydrophobic photolabeling method to study the noncovalent interactions between plasma membrane calcium pump (PMCA) and surrounding phospholipids. With this approach, we determined (1) the number of lipid molecules in close contact with the transmembrane surface, i.e., the lipid-protein stoichiometry, and (2) the distribution of lipid molecules among different regions of the protein. PMCA was photolabeled in mixed micelles containing detergent, the phosphatidylcholine photoactivatable analog 1-palmitoyl-2-[9-[2'-[125I]iodo-4'- (trifluoromethyldiazirinyl)-benzyloxycarbonyl]-nonaoyl]-sn-glycero-3-phosphocholine, and different amounts of dimyristoyl phosphatidylcholine (PC). The stoichiometry was estimated after the extent of the labeling reaction had been independently assessed. We determined a maximum number of 17 +/- 1 molecules of PC in close contact with the transmembrane surface per PMCA molecule. In addition, a semiquantitative description of the phospholipid environment around different regions of PMCA was carried out after limited proteolysis of the photolabeled protein. The distribution of labels among the N-terminal (1-322), the central (323-660), and the C-terminal (661-1,205) regions was 26, 36, and 38%, respectively.

journal_name

Cell Biochem Biophys

authors

Villamil Giraldo AM,Castello PR,González Flecha FL,Delfino JM,Rossi JP

doi

10.1385/cbb:44:3:431

subject

Has Abstract

pub_date

2006-01-01 00:00:00

pages

431-7

issue

3

eissn

1085-9195

issn

1559-0283

pii

CBB:44:3:431

journal_volume

44

pub_type

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