@article{ETD,
      recid = {2180},
      author = {Scott, Gregory},
      title = {Regulation of PACS-1-directed protein trafficking},
      publisher = {Oregon Health and Science University},
      school = {Ph.D.},
      address = {2006},
      number = {ETD},
      abstract = {The cation-independent mannose-6-phosphate receptor  (CI-MPR) cycles between the trans-Golgi network and  endosomes to mediate lysosomal hydrolase trafficking, a  process regulated by the adaptor proteins GGA3 and PACS-1.  Although both bind a CK2-phosphorylated acidic cluster  motif on CI-MPR, they direct opposing sorting steps. This  study identifies autoregulatory acidic cluster domains in  PACS-1 and GGA3 that are differentially controlled by CK2  phosphorylation. PACS-1 links CK2 to GGA3, forming a  complex that coordinates CI-MPR release, retrieval, and  recycling. These findings reveal a CK2-driven  phosphorylation cascade that orchestrates endosomal–Golgi  protein trafficking.},
      url = {http://digitalcollections.ohsu.edu/record/2180},
      doi = {https://doi.org/10.6083/M44X562N},
}