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TitleStructural basis of an endocytic checkpoint that primes the AP2 clathrin adaptor for cargo internalization.
Journal, issue, pagesNat Struct Mol Biol, Vol. 29, Issue 4, Page 339-347, Year 2022
Publish dateMar 28, 2022
AuthorsEdward A Partlow / Kevin S Cannon / Gunther Hollopeter / Richard W Baker /
PubMed AbstractClathrin-mediated endocytosis (CME) is the main route of internalization from the plasma membrane. It is known that the heterotetrameric AP2 clathrin adaptor must open to simultaneously engage ...Clathrin-mediated endocytosis (CME) is the main route of internalization from the plasma membrane. It is known that the heterotetrameric AP2 clathrin adaptor must open to simultaneously engage membrane and endocytic cargo, yet it is unclear how transmembrane cargos are captured to catalyze CME. Using cryogenic-electron microscopy, we discover a new way in which mouse AP2 can reorganize to expose membrane- and cargo-binding pockets, which is not observed in clathrin-coated structures. Instead, it is stimulated by endocytic pioneer proteins called muniscins, which do not enter vesicles. Muniscin-engaged AP2 is primed to rearrange into the vesicle-competent conformation on binding the tyrosine cargo internalization motif (YxxΦ). We propose adaptor priming as a checkpoint to ensure cargo internalization.
External linksNat Struct Mol Biol / PubMed:35347313 / PubMed Central
MethodsEM (single particle)
Resolution3.5 - 4.7 Å
Structure data

24710

7rw8

EMDB-24710, PDB-7rw8:
AP2 bound to heparin in the closed conformation
Method: EM (single particle) / Resolution: 3.5 Å

24711

7rw9

EMDB-24711, PDB-7rw9:
AP2 bound to heparin in the bowl conformation
Method: EM (single particle) / Resolution: 3.9 Å

24712

7rwa

EMDB-24712, PDB-7rwa:
AP2 bound to heparin and Tgn38 tyrosine cargo peptide
Method: EM (single particle) / Resolution: 4.7 Å

24713

7rwb

EMDB-24713, PDB-7rwb:
AP2 bound to the APA domain of SGIP in the presence of heparin
Method: EM (single particle) / Resolution: 3.9 Å

24714

7rwc

EMDB-24714, PDB-7rwc:
AP2 bound to the APA domain of SGIP and heparin; partial signal subtraction and symmetry expansion
Method: EM (single particle) / Resolution: 3.8 Å

Source
  • mus musculus (house mouse)
KeywordsENDOCYTOSIS / AP2 / clathrin vesicle / lipid-binding / adaptor / membrane / transport / cargo / muniscin / regulator / SGIP1

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