Comprehensive proteomic analysis of nonintegrin laminin receptor interacting proteins.
Human nonintegrin laminin receptor is a multifunctional protein acting as an integral component of the ribosome and a cell surface receptor for laminin-1. The laminin receptor is overexpressed in several human cancers and is also the cell surface receptor for several viruses and pathogenic prion proteins, making it a pathologically significant protein. This study focused on the proteomic characterization of laminin receptor interacting proteins from Mus musculus. The use of affinity chromatography with immobilized recombinant laminin receptor coupled with mass spectrometry analysis identified 45 proteins with high confidence. Following validation through coimmunoprecipitation, the proteins were classified based on predicted function into ribosomal, RNA processing, signal transduction/metabolism, protein processing, cytoskeleton/cell anchorage, DNA/chromatin, and unknown functions. A significant portion of the identified proteins is related to functions or localizations previously described for laminin receptor. This work represents a comprehensive proteomic approach to studying laminin receptor and provides an essential stepping stone to a better mechanistic understanding of this protein's diverse functions.
Gene Therapy Center, Cancer Institute and Department of Pathology, New York University School of Medicine, 550 First Avenue, New York, New York 10016, United States.
Lisa
L
Venticinque
Daniel
D
Meruelo
D000818:Animals; D056404:Chaperonin Containing TCP-1 / Q000737:chemistry / Q000302:isolation & purification; D002846:Chromatography, Affinity; D003598:Cytoskeletal Proteins / Q000737:chemistry / Q000302:isolation & purification; D006602:Hexosyltransferases; D006657:Histones / Q000737:chemistry / Q000302:isolation & purification; D006801:Humans; D047908:Intracellular Signaling Peptides and Proteins / Q000737:chemistry / Q000302:isolation & purification; D051379:Mice; D041681:NIH 3T3 Cells; D046988:Proteasome Endopeptidase Complex / Q000737:chemistry / Q000302:isolation & purification; D011485:Protein Binding; D020543:Proteome / Q000737:chemistry* / Q000302:isolation & purification; D040901:Proteomics; D016601:RNA-Binding Proteins / Q000737:chemistry / Q000302:isolation & purification; D017474:Receptors, Laminin / Q000737:chemistry; D012269:Ribosomal Proteins / Q000737:chemistry / Q000302:isolation & purification; D014157:Transcription Factors / Q000737:chemistry / Q000302:isolation & purification
D003598:Cytoskeletal Proteins; D006657:Histones; D047908:Intracellular Signaling Peptides and Proteins; D020543:Proteome; D016601:RNA-Binding Proteins; C510624:RPSA protein, human; D017474:Receptors, Laminin; D012269:Ribosomal Proteins; C101681:SMARCC1 protein, human; D014157:Transcription Factors; D006602:Hexosyltransferases; C517590:RPN2 protein, human; D046988:Proteasome Endopeptidase Complex; D056404:Chaperonin Containing TCP-1