0B68 Wedegaertner, Philip B. - Thomas Jefferson University - Thomas Jefferson University

Philip B. Wedegaertner, PhD

Contact Dr. Wedegaertner

233 S. 10th St.
839 BLSB
Philadelphia, PA 19107

(215) 503-3137

Most Recent Peer-reviewed Publications

  1. Leukemia-associated RhoGEF (LARG) is a novel RhoGEF in cytokinesis and required for the proper completion of abscission
  2. G protein trafficking.
  3. Non-canonical signaling and localizations of heterotrimeric G proteins
  4. Reversible palmitoylation in g protein signaling
  5. Regulation of constitutive cargo transport from the trans-Golgi network to plasma membrane by Golgi-localized G protein βγ subunits
  6. An N-terminal polybasic motif of Gαq is required for signaling and influences membrane nanodomain distribution
  7. The amino acid motif L/IIxxFE defines a novel actin-binding sequence in PDZ-RhoGEF
  8. Differences in Gα12- and Gα13-mediated plasma membrane recruitment of p115-RhoGEF
  9. N-terminal polybasic motifs are required for plasma membrane localization of Gαs and Gαq
  10. FAK, PDZ-RhoGEF and ROCKII cooperate to regulate adhesion movement and trailing-edge retraction in fibroblasts
  11. Disruption of oligomerization induces nucleocytoplasmic shuttling of leukemia-associated Rho guanine-nucleotide exchange factor
  12. Plasma membrane and nuclear localization of G protein-coupled receptor kinase 6A
  13. Assembly and trafficking of heterotrimeric G proteins
  14. Lipid-protein interactions in GPCR-associated signaling
  15. Cooperative regulation of p70S6 kinase by receptor tyrosine kinases and G protein-coupled receptors augments airway smooth muscle growth
  16. Loss of association between activated Gαq and Gβγ disrupts receptor-dependent and receptor-independent signaling
  17. Functional consequences of Gα13 mutations that disrupt interaction with p115RhoGEF
  18. Identification of a specific domain responsible for JNK2α2 autophosphorylation
  19. Palmitoylation and plasma membrane targeting of RGS7 are promoted by αo
  20. Characterization of the GRK2 binding site of Gαq