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Clathrin assembly protein AP180: primary structure, domain organization and identification of a clathrin binding site.
Author(s) -
Morris S.A.,
Schröder S.,
Plessmann U.,
Weber K.,
Ungewickell E.
Publication year - 1993
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1993.tb05700.x
Subject(s) - biology , clathrin , binding site , clathrin adaptor proteins , plasma protein binding , computational biology , microbiology and biotechnology , biochemistry , endocytosis , receptor
Binding of AP180 to clathrin triskelia induces their assembly into 60‐70 nm coats. The largest rat brain cDNA clone isolated predicts a molecular weight of 91,430 for AP180. Two cDNA clones have an additional small 57 bp insert. The deduced molecular weight agrees with gel filtration results provided the more chaotropic denaturant 6 M guanidinium thiocyanate is substituted for the weaker guanidinium chloride. The sequence and the proteolytic cleavage pattern suggest a three domain structure. The N‐terminal 300 residues (pI 8.7) harbour a clathrin binding site. An acidic middle domain (pI 3.6, 450 residues), interrupted by an uncharged alanine rich segment of 59 residues, appears to be responsible for the anomalous physical properties of AP180. The C‐terminal domain (166 residues) has a pI of 10.4. AP180 mRNA is restricted to neuronal sources. AP180 shows no significant homology to known clathrin binding proteins, but is nearly identical to a mouse phosphoprotein (F1‐20). This protein, localized to synaptic termini, has so far been of unknown function.