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TitlePICK1 is implicated in organelle motility in an Arp2/3 complex-independent manner.
Journal, issue, pagesMol Biol Cell, Vol. 26, Issue 7, Page 1308-1322, Year 2015
Publish dateApr 1, 2015
AuthorsYadaiah Madasu / Changsong Yang / Malgorzata Boczkowska / Kelley A Bethoney / Adam Zwolak / Grzegorz Rebowski / Tatyana Svitkina / Roberto Dominguez /
PubMed AbstractPICK1 is a modular scaffold implicated in synaptic receptor trafficking. It features a PDZ domain, a BAR domain, and an acidic C-terminal tail (ACT). Analysis by small- angle x-ray scattering ...PICK1 is a modular scaffold implicated in synaptic receptor trafficking. It features a PDZ domain, a BAR domain, and an acidic C-terminal tail (ACT). Analysis by small- angle x-ray scattering suggests a structural model that places the receptor-binding site of the PDZ domain and membrane-binding surfaces of the BAR and PDZ domains adjacent to each other on the concave side of the banana-shaped PICK1 dimer. In the model, the ACT of one subunit of the dimer interacts with the PDZ and BAR domains of the other subunit, possibly accounting for autoinhibition. Consistently, full-length PICK1 shows diffuse cytoplasmic localization, but it clusters on vesicle-like structures that colocalize with the trans-Golgi network marker TGN38 upon deletion of either the ACT or PDZ domain. This localization is driven by the BAR domain. Live-cell imaging further reveals that PICK1-associated vesicles undergo fast, nondirectional motility in an F-actin-dependent manner, but deleting the ACT dramatically reduces vesicle speed. Thus the ACT links PICK1-associated vesicles to a motility factor, likely myosin, but, contrary to previous reports, PICK1 neither binds nor inhibits Arp2/3 complex.
External linksMol Biol Cell / PubMed:25657323 / PubMed Central
MethodsSAS (X-ray synchrotron)
Structure data

SASDBL2:
MBP-PICK1 fusion (Maltose Binding Protein fused to Protein Interacting with C kinase 1, MBP-PICK1)
Method: SAXS/SANS

Source
  • Homo sapiens (human)

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