title: Discoidin domain receptors: unique receptor tyrosine kinases in collagen-mediated signaling.
abstract: The discoidin domain receptors (DDRs) are receptor tyrosine kinases that recognize collagens as their ligands. DDRs display unique structural features and distinctive activation kinetics, which set them apart from other members of the kinase superfamily. DDRs regulate cell-collagen interactions in normal and pathological conditions and thus are emerging as major sensors of collagen matrices and potential novel therapeutic targets. New structural and biological information has shed light on the molecular mechanisms that regulate DDR signaling, turnover, and function. This minireview provides an overview of these areas of DDR research with the goal of fostering further investigation of these intriguing and unique receptors.
authors: Department of Pathology, School of Medicine, Wayne State University, Detroit, Michigan 48201.
authors: Hsueh-Liang
authors: HL
authors: Fu
authors: Department of Pathology, School of Medicine, Wayne State University, Detroit, Michigan 48201.
authors: Rajeshwari R
authors: RR
authors: Valiathan
authors: Department of Pathology, School of Medicine, Wayne State University, Detroit, Michigan 48201.
authors: Richard
authors: R
authors: Arkwright
authors: Department of Pathology, School of Medicine, Wayne State University, Detroit, Michigan 48201.
authors: Anjum
authors: A
authors: Sohail
authors: Davis Heart and Lung Research Institute and Biomedical Engineering Department, Ohio State University, Columbus, Ohio 43210.
authors: Cosmin
authors: C
authors: Mihai
authors: Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana 46556.
authors: Malika
authors: M
authors: Kumarasiri
authors: Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana 46556.
authors: Kiran V
authors: KV
authors: Mahasenan
authors: Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana 46556.
authors: Shahriar
authors: S
authors: Mobashery
authors: Institute of Cancer Research, Chester Beatty Laboratories, London SW3 6JB, United Kingdom.
authors: Paul
authors: P
authors: Huang
authors: Davis Heart and Lung Research Institute and Biomedical Engineering Department, Ohio State University, Columbus, Ohio 43210.
authors: Gunjan
authors: G
authors: Agarwal
authors: Department of Pathology, School of Medicine, Wayne State University, Detroit, Michigan 48201. Electronic address: rfridman@med.wayne.edu.
authors: Rafael
authors: R
authors: Fridman
mesh_terms: D000818:Animals; D003094:Collagen / Q000737:chemistry; D000070818:Discoidin Domain Receptors; D004705:Endocytosis; D005109:Extracellular Matrix / Q000378:metabolism; D005786:Gene Expression Regulation; D006801:Humans; D007700:Kinetics; D008024:Ligands; D051379:Mice; D008958:Models, Molecular; D008968:Molecular Conformation; D010447:Peptide Hydrolases / Q000737:chemistry; D019000:Phosphotyrosine / Q000737:chemistry; D017434:Protein Structure, Tertiary; D020794:Receptor Protein-Tyrosine Kinases / Q000737:chemistry / Q000378:metabolism*; D011975:Receptors, Mitogen / Q000737:chemistry*; D015398:Signal Transduction
chemical_list: D008024:Ligands; D011975:Receptors, Mitogen; D019000:Phosphotyrosine; D003094:Collagen; D000070818:Discoidin Domain Receptors; D020794:Receptor Protein-Tyrosine Kinases; D010447:Peptide Hydrolases