Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Publication

Huntingtin interacting protein 1 (HIP1) regulates clathrin assembly through direct binding to the regulatory region of the clathrin light chain.

Legendre-Guillemin V, Metzler M, Lemaire JF, Philie J, Gan L, Hayden MR, McPherson PS

Huntingtin interacting protein 1 (HIP1) is a component of clathrin coats. We previously demonstrated that HIP1 promotes clathrin assembly through its central helical domain, which binds directly to clathrin light chains (CLCs). To better understand the relationship between CLC binding and clathrin assembly we sought to dissect this interaction. Using C-terminal deletion constructs of the HIP1 helical domain, we identified ... [more]

J. Biol. Chem. Feb. 18, 2005; 280(7);6101-8 [Pubmed: 15533941]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
HIP1 CLTB
Co-crystal Structure
Co-crystal Structure

Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.

Low-BioGRID
-
CLTB HIP1
Proximity Label-MS
Proximity Label-MS

An interaction is inferred when a bait-enzyme fusion protein selectively modifies a vicinal protein with a diffusible reactive product, followed by affinity capture of the modified protein and identification by mass spectrometric methods.

High85BioGRID
2983582
CLTB HIP1
Reconstituted Complex
Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Low-BioGRID
-
HIP1 CLTB
Reconstituted Complex
Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Low-BioGRID
-

Curated By

  • BioGRID