Emerging roles of post-translational modifications in signal transduction and angiogenesis

• Published in: Proteomics (Weinheim) Vol. 15; no. 2-3; pp. 300 - 309
• Main Authors: Rahimi, Nader, Costello, Catherine E.
• Format: Journal Article
• Language: English
• Published: Germany Blackwell Publishing Ltd 01.01.2015; Wiley Subscription Services, Inc
• Subjects: Acetylation; Amino Acid Sequence; Angiogenesis; Animals; Cell biology; Cell differentiation; Cell migration; Differentiation (biology); Endothelial cells; Glycosylation; Humans; Kinases; Methylation; Models, Molecular; Molecular Sequence Data; Neovascularization, Pathologic - metabolism; Neovascularization, Physiologic; Permeability; Phosphorylation; Protein Processing, Post-Translational; Signal Transduction; Signaling; Tandem mass spectrometry; Tyrosine; Ubiquitination; Vascular endothelial growth factor; Vascular Endothelial Growth Factor Receptor-2 - analysis; Vascular Endothelial Growth Factor Receptor-2 - metabolism; Vascular endothelial growth factor receptors; VEGF receptor; Cell biology; Tandem mass spectrometry; Phosphorylation; Glycosylation; Acetylation; VEGF receptor
• ISSN: 1615-9853; 1615-9861; 1615-9861
• DOI: 10.1002/pmic.201400183

The vascular endothelial growth factor receptor‐2 (VEGFR‐2) belongs to the family of receptor tyrosine kinases and is a key player in vasculogenesis and pathological angiogenesis. An emerging picture of PTMs of VEGFR‐2 suggests that they play central roles in generating a highly dynamic and complex...