Switches.ELM

Switch #:

SWTI000677

Description:
Amphiphysin 1 contains two distinct motifs that bind to distinct sites on N-terminal beta-propeller domain of clathrin, resulting in increased binding strength to free domain. This, in combination with binding of its BAR domain to curved membranes, results in localisation of amphipysin to the periphery of the assembling clathrin lattice. The two clathrin-binding motifs are regulated by phosphorylation of adjacent modification sites (see switch details and switch details).

Participants:
(1) Amphiphysin (AMPH)
(2) Clathrin heavy chain 1 (CLTC)

Interactions

Interaction #1 AMPH - CLTC

Interfaces
(1) LIG_Clathr_ClatBox_1 motif (₃₅₁LLDLD₃₅₅) in Amphiphysin (AMPH)
(2) Clathrin propeller repeat_(19-56) and _(148-187) and _(198-234) in Clathrin heavy chain 1 (CLTC)
Additional Information
Affinity : W-box peptide: 28 µM, clathrin-box peptide: 22 µM, W-box + clathrin-box peptide: =<5 µM

Interaction #2 AMPH - CLTC

Interfaces
(3) LIG_Clathr_ClatBox_2 motif (₃₈₀LPWDLW₃₈₅) in Amphiphysin (AMPH)
(4) Clathrin propeller repeat_(19-56) and _(148-187) and _(198-234) in Clathrin heavy chain 1 (CLTC)
Additional Information
Affinity : W-box peptide: 28 µM, clathrin-box peptide: 22 µM, W-box + clathrin-box peptide: =<5 µM

Context

Switch localisation
Curated: clathrin coat
ELM curated: cytoskeleton, Golgi apparatus, cytosol, Golgi trans-face, clathrin-coated endocytic vesicle

References

(1) Two distinct interaction motifs in amphiphysin bind two independent sites on the clathrin terminal domain beta-propeller.
Miele et al. Nat. Struct. Mol. Biol. (2004)