Protein-Phospholipid Interactions in Nonclassical Protein Secretion: Problem and Methods of Study

International Journal of Molecular Sciences

Igor Prudovsky³  Thallapuranam Krishnaswamy Suresh Kumar¹  Sarah Sterling² 

[1] Department of Chemistry and Biochemistry, University of Arkansas, Fayetteville, AR 72701, USA; E-Mail:;Department of Chemical and Biological Engineering, University of Maine, Orono, ME 04469, USA; E-Mails:;Maine Medical Center Research Institute, 81 Research Drive, Scarborough, ME 04074, USA

关键词: FGF;    phospholipid;    nonclassical secretion;    S100A13;    sphingosine kinase 1;    annexin 2;    phospholipid;    SFS;    FCS;    liposome;    supported bilayer;    copper;    synaptotagmin 1;   

DOI  :  10.3390/ijms14023734

来源: mdpi

【 摘 要 】

Extracellular proteins devoid of signal peptides use nonclassical secretion mechanisms for their export. These mechanisms are independent of the endoplasmic reticulum and Golgi. Some nonclassically released proteins, particularly fibroblast growth factors (FGF) 1 and 2, are exported as a result of their direct translocation through the cell membrane. This process requires specific interactions of released proteins with membrane phospholipids. In this review written by a cell biologist, a structural biologist and two membrane engineers, we discuss the following subjects: (i) Phenomenon of nonclassical protein release and its biological significance; (ii) Composition of the FGF1 multiprotein release complex (MRC); (iii) The relationship between FGF1 export and acidic phospholipid externalization; (iv) Interactions of FGF1 MRC components with acidic phospholipids; (v) Methods to study the transmembrane translocation of proteins; (vi) Membrane models to study nonclassical protein release.

【 授权许可】

CC BY   
© 2013 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland.