Member database | Pfam |
Pfam type | repeat |
Short name | Sec10_N |
Clan | TPR |
Author | Chuguransky S;0000-0002-0520-0736 |
Sequence Ontology | 0001068 |
Description
This entry contains the Sec10 component (approximately 650 residues long) of the eukaryotic exocyst complex, which mediates the tethering of post-Golgi secretory vesicles to the plasma membrane and promotes the assembly of the SNARE complex for membrane fusion. It is also involved in cell polarisation, primary ciliogenesis, cytokinesis, pathogen invasion, tumourigenesis and metastasis
[2, 1]. The exocyst is a member of the Complex Associated with Tethering Containing Helical Rods (CATCHRs) which also includes DSL1, COG and GARP complexes, evolutionary related. They share structural features comprising alpha-helical bundles towards the C-terminal and coiled-coil regions at the N-terminal. This entry represents the N-terminal coiled-coil region (also referred to as CorEx motif) of Sec10 and its homologues from animals ECOC5 (Exocyst complex component 5), which participates in the central pair-wise interactions by forming an intact antiparallel 'zipper' which Sec15 subunit. Sec10-Sec15 CorEx motifs interact with Exo70-Exo84 dimers and form a four-helical bundle
[3].
References
1.Crystal structure of Sec10, a subunit of the exocyst complex. Chen J, Yamagata A, Kubota K, Sato Y, Goto-Ito S, Fukai S. Sci Rep 7, 40909, (2017). PMID: 28098232
2.The exocyst affects protein synthesis by acting on the translocation machinery of the endoplasmic reticulum. Lipschutz JH, Lingappa VR, Mostov KE. J. Biol. Chem. 278, 20954-60, (2003). View articlePMID: 12665531
Further reading
4. Homology and Modular Evolution of CATCHR at the Origin of the Eukaryotic Endomembrane System. Santana-Molina C, Gutierrez F, Devos DP. Genome Biol Evol 13, (2021). PMID: 34061181