BAIT

SYNE1

8B, ARCA1, C6orf98, CPG2, EDMD4, MYNE1, Nesp1, SCAR8, dJ45H2.2, RP1-130E4.2
spectrin repeat containing, nuclear envelope 1
Glioblastoma Project
Homo sapiens
PREY

SUN2

UNC84B, RP3-508I15.15-002
Sad1 and UNC84 domain containing 2
Homo sapiens

Affinity Capture-Western

An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.

Publication

LINC complexes form by binding of three KASH peptides to domain interfaces of trimeric SUN proteins.

Sosa BA, Rothballer A, Kutay U, Schwartz TU

Linker of nucleoskeleton and cytoskeleton (LINC) complexes span the nuclear envelope and are composed of KASH and SUN proteins residing in the outer and inner nuclear membrane, respectively. LINC formation relies on direct binding of KASH and SUN in the perinuclear space. Thereby, molecular tethers are formed that can transmit forces for chromosome movements, nuclear migration, and anchorage. We present ... [more]

Cell May. 25, 2012; 149(5);1035-47 [Pubmed: 22632968]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
SUN2 SYNE1
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
-

Curated By

  • BioGRID