BIOMAT Database Logo BIOMAT Database Logo

Binding of GAPR-1 to negatively charged phospholipid membranes: unusual binding characteristics to phosphatidylinositol. 2010

Josse Van Galen, and Bas W M Van Balkom, and Ramon L Serrano, and Dora Kaloyanova, and Ruud Eerland, and Ernstpeter Stüven, and J Bernd Helms
Department of Biochemistry and Cell Biology and Institute of Biomembranes, Utrecht University, Utrecht.

Golgi-Associated Plant Pathogenesis-Related protein 1 (GAPR-1) is a mammalian protein that belongs to the superfamily of plant pathogenesis-related proteins group 1 (PR-1). GAPR-1 strongly associates with lipid rafts at the cytosolic leaflet of the Golgi membrane. The myristoyl moiety at the N-terminus of GAPR-1 contributes to membrane binding but is not sufficient for stable membrane anchorage. GAPR-1 is positively charged at physiological pH, which allows for additional membrane interactions with proteins or lipids. To determine the potential contribution of lipids to membrane binding of GAPR-1, we used a liposome binding assay. Here we report that non-myristoylated GAPR-1 stably binds liposomes that contain the negatively charged lipids phosphatidylserine, phosphatidylglycerol, phosphatidylinositol, or phosphatidic acid. GAPR-1 displays the highest preference for phosphatidic acid-containing liposomes. In contrast, lysozyme, which contains a similar surface charge, did not bind to these liposomes, except for a weak membrane association with PA-containing liposomes. Interestingly, GAPR-1 binds to phosphatidylinositol with unusual characteristics. Denaturation or organic extraction of GAPR-1 does not result in dissociation of phosphatidylinositol from GAPR-1. The association of phosphatidylinositol with GAPR-1 results in a diffuse gel-shift in SDS-PAGE. Mass spectrometric analysis of gel-shifted GAPR-1 showed the association of up to 3 molecules of phosphatidylinositol with GAPR-1. These results suggest that the lipid composition contributes to the GAPR-1 binding to biological membranes.

UI MeSH Term Description Entries
D008565 Membrane Proteins Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors. Cell Membrane Protein,Cell Membrane Proteins,Cell Surface Protein,Cell Surface Proteins,Integral Membrane Proteins,Membrane-Associated Protein,Surface Protein,Surface Proteins,Integral Membrane Protein,Membrane Protein,Membrane-Associated Proteins,Membrane Associated Protein,Membrane Associated Proteins,Membrane Protein, Cell,Membrane Protein, Integral,Membrane Proteins, Integral,Protein, Cell Membrane,Protein, Cell Surface,Protein, Integral Membrane,Protein, Membrane,Protein, Membrane-Associated,Protein, Surface,Proteins, Cell Membrane,Proteins, Cell Surface,Proteins, Integral Membrane,Proteins, Membrane,Proteins, Membrane-Associated,Proteins, Surface,Surface Protein, Cell
D010716 Phosphatidylinositols Derivatives of phosphatidic acids in which the phosphoric acid is bound in ester linkage to the hexahydroxy alcohol, myo-inositol. Complete hydrolysis yields 1 mole of glycerol, phosphoric acid, myo-inositol, and 2 moles of fatty acids. Inositide Phospholipid,Inositol Phosphoglyceride,Inositol Phosphoglycerides,Inositol Phospholipid,Phosphoinositide,Phosphoinositides,PtdIns,Inositide Phospholipids,Inositol Phospholipids,Phosphatidyl Inositol,Phosphatidylinositol,Inositol, Phosphatidyl,Phosphoglyceride, Inositol,Phosphoglycerides, Inositol,Phospholipid, Inositide,Phospholipid, Inositol,Phospholipids, Inositide,Phospholipids, Inositol
D011485 Protein Binding The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. Plasma Protein Binding Capacity,Binding, Protein
D002462 Cell Membrane The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells. Plasma Membrane,Cytoplasmic Membrane,Cell Membranes,Cytoplasmic Membranes,Membrane, Cell,Membrane, Cytoplasmic,Membrane, Plasma,Membranes, Cell,Membranes, Cytoplasmic,Membranes, Plasma,Plasma Membranes
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D013696 Temperature The property of objects that determines the direction of heat flow when they are placed in direct thermal contact. The temperature is the energy of microscopic motions (vibrational and translational) of the particles of atoms. Temperatures
D013997 Time Factors Elements of limited time intervals, contributing to particular results or situations. Time Series,Factor, Time,Time Factor

Related Publications

Josse Van Galen, and Bas W M Van Balkom, and Ramon L Serrano, and Dora Kaloyanova, and Ruud Eerland, and Ernstpeter Stüven, and J Bernd Helms
Binding of monovalent alkali metal ions with negatively charged phospholipid membranes.
April 2016, Biochimica et biophysica acta,
Josse Van Galen, and Bas W M Van Balkom, and Ramon L Serrano, and Dora Kaloyanova, and Ruud Eerland, and Ernstpeter Stüven, and J Bernd Helms
Binding of a fluorescent dansylcadaverine-substance P analogue to negatively charged phospholipid membranes.
July 2000, International journal of biological macromolecules,
Josse Van Galen, and Bas W M Van Balkom, and Ramon L Serrano, and Dora Kaloyanova, and Ruud Eerland, and Ernstpeter Stüven, and J Bernd Helms
Cations induce shape remodeling of negatively charged phospholipid membranes.
June 2017, Physical chemistry chemical physics : PCCP,
Josse Van Galen, and Bas W M Van Balkom, and Ramon L Serrano, and Dora Kaloyanova, and Ruud Eerland, and Ernstpeter Stüven, and J Bernd Helms
Covalent binding of negatively charged phospholipid to Na,K-ATPase.
January 1984, Biochemistry international,
Josse Van Galen, and Bas W M Van Balkom, and Ramon L Serrano, and Dora Kaloyanova, and Ruud Eerland, and Ernstpeter Stüven, and J Bernd Helms
Transient high affinity binding of tissue factor pathway inhibitor-factor Xa complexes to negatively charged phospholipid membranes.
March 1998, Biochemistry,
Josse Van Galen, and Bas W M Van Balkom, and Ramon L Serrano, and Dora Kaloyanova, and Ruud Eerland, and Ernstpeter Stüven, and J Bernd Helms
Binding of β-amyloid (1-42) peptide to negatively charged phospholipid membranes in the liquid-ordered state: modeling and experimental studies.
August 2012, Biophysical journal,
Josse Van Galen, and Bas W M Van Balkom, and Ramon L Serrano, and Dora Kaloyanova, and Ruud Eerland, and Ernstpeter Stüven, and J Bernd Helms
Evidence from total internal reflection fluorescence microscopy for calcium-independent binding of prothrombin to negatively charged planar phospholipid membranes.
November 1991, Biochemistry,
Josse Van Galen, and Bas W M Van Balkom, and Ramon L Serrano, and Dora Kaloyanova, and Ruud Eerland, and Ernstpeter Stüven, and J Bernd Helms
The interaction of neuropeptide Y with negatively charged and zwitterionic phospholipid membranes.
June 2009, European biophysics journal : EBJ,
Josse Van Galen, and Bas W M Van Balkom, and Ramon L Serrano, and Dora Kaloyanova, and Ruud Eerland, and Ernstpeter Stüven, and J Bernd Helms
Calcium-dependent binding of uteroglobin (PCB-BP/CCSP) to negatively charged phospholipid liposomes.
November 1995, FEBS letters,
Josse Van Galen, and Bas W M Van Balkom, and Ramon L Serrano, and Dora Kaloyanova, and Ruud Eerland, and Ernstpeter Stüven, and J Bernd Helms
Binding of crotoxin, a presynaptic phospholipase A2 neurotoxin, to negatively charged phospholipid vesicles.
October 1989, Journal of neurochemistry,
Copied contents to your clipboard!