Functional Organization of Clathrin in Coats
1999; Elsevier BV; Volume: 3; Issue: 6 Linguagem: Inglês
10.1016/s1097-2765(01)80008-3
ISSN1097-4164
AutoresAndrea Musacchio, Corinne J. Smith, Alan M. Roseman, Stephen C. Harrison, Tomas Kirchhausen, Barbara M. F. Pearse,
Tópico(s)Surface Modification and Superhydrophobicity
ResumoThe sorting of specific proteins into clathrin-coated pits and the mechanics of membrane invagination are determined by assembly of the clathrin lattice. Recent structures of a six-fold barrel clathrin coat at 21 Å resolution by electron cryomicroscopy and of the clathrin terminal domain and linker at 2.6 Å by X-ray crystallography together show how domains of clathrin interact and orient within the coat and reveal the strongly puckered shape and conformational variability of individual triskelions. The β propeller of the terminal domain faces the membrane so that recognition segments from adaptor proteins can extend along its lateral grooves. Clathrin legs adapt to different coat environments in the barrel by flexing along a segment at the knee that is free of contacts with other molecules.
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