Faculty Collaboration Database

Structural studies of apoptosis and ion transport regulatory proteins in membranes. Magn Reson Chem 2004 Feb;42(2):172-9

Date

01/28/2004

Pubmed ID

14745797

Pubmed Central ID

PMC3033199

DOI

10.1002/mrc.1322

Scopus ID

2-s2.0-0842264375 (requires institutional sign-in at Scopus site)   41 Citations

Abstract

Solid-state NMR spectroscopy is being used to determine the structures of membrane proteins involved in the regulation of apoptosis and ion transport. The Bcl-2 family includes pro- and anti-apoptotic proteins that play a major regulatory role in mitochondrion-dependent apoptosis or programmed cell death. The NMR data obtained for (15)N-labeled anti-apoptotic Bcl-xL in lipid bilayers are consistent with membrane association through insertion of the two central hydrophobic alpha-helices that are also required for channel formation and cytoprotective activity. The FXYD family proteins regulate ion flux across membranes, through interaction with the Na(+), K(+)-ATPase, in tissues that perform fluid and solute transport or that are electrically excitable. We have expressed and purified three FXYD family members, Mat8 (mammary tumor protein), CHIF (channel-inducing factor) and PLM (phospholemman), for structure determination by NMR in lipids. The solid-state NMR spectra of Bcl-2 and FXYD proteins, in uniaxially oriented lipid bilayers, give the first view of their membrane-associated architectures.

Author List

Franzin CM, Choi J, Zhai D, Reed JC, Marassi FM

Author

Francesca M. Marassi PhD Chair, Professor in the Biophysics department at Medical College of Wisconsin

MESH terms used to index this publication - Major topics in bold

Amino Acid Sequence
Apoptosis
Cloning, Molecular
Conserved Sequence
Humans
Lipid Bilayers
Magnetic Resonance Spectroscopy
Membrane Proteins
Models, Molecular
Neoplasm Proteins
Protein Conformation
Protein Structure, Secondary
Proto-Oncogene Proteins c-bcl-2
Recombinant Proteins