PUBLICATION

The C7orf43/TRAPPC14 component links the TRAPPII complex to RABIN8 for preciliary vesicle tethering at the mother centriole during ciliogenesis

Authors
Cuenca, A., Insinna, C., Zhao, H., John, P., Weiss, M.A., Lu, Q., Walia, V., Specht, S., Manivannan, S., Stauffer, J., Peden, A.A., Westlake, C.J.
ID
ZDB-PUB-190902-4
Date
2019
Source
The Journal of biological chemistry   294(42): 15418-15434 (Journal)
Registered Authors
Keywords
Rab, Rabin8, TRAPPII complex, centrosome, cilia, ciliogenesis, intracellular trafficking, membrane trafficking, mother centriole
MeSH Terms
  • Animals
  • Centrioles/genetics
  • Centrioles/metabolism*
  • Cilia/genetics
  • Cilia/metabolism*
  • Cytoplasmic Vesicles/genetics
  • Cytoplasmic Vesicles/metabolism*
  • Germinal Center Kinases/genetics
  • Germinal Center Kinases/metabolism*
  • Humans
  • Morphogenesis
  • Protein Binding
  • Zebrafish
PubMed
31467083 Full text @ J. Biol. Chem.
Abstract
The primary cilium is a cellular sensor that detects light, chemicals, and movement and is important for morphogen and growth factor signaling. The small GTPase RAB11, member RAS oncogene family (RAB11)-RAB8 cascade is required for ciliogenesis. RAB11 traffics the guanine nucleotide exchange factor (GEF) RABIN8 to the centrosome to activate RAB8, needed for ciliary growth. RABIN8 also requires the transport particle protein complex (TRAPPC) proteins for centrosome recruitment during ciliogenesis. Here, using an MS-based approach for identifying RABIN8-interacting proteins, we identified C7orf43 (also known as microtubule-associated Protein 11 [MAP11]) as being required for ciliation both in human cells and zebrafish embryos. We found that C7orf43 directly binds to RABIN8 and that C7orf43 knockdown diminishes RABIN8 preciliary centrosome accumulation. Interestingly, we found that C7orf43 co-sediments with TRAPPII complex subunits and directly interacts with TRAPPC proteins. Our findings establish that C7orf43 is a TRAPPII-specific complex component, referred to here as TRAPPC14. Additionally, we show that TRAPPC14 is dispensable for TRAPPII complex integrity, but mediates RABIN8 association with the TRAPPII complex. Finally, we demonstrate that TRAPPC14 interacts with the distal appendage proteinsFas-binding factor 1 (FBF1) and centrosomal protein 83 (CEP83), which we show here are required for GFP-RABIN8 centrosomal accumulation, supporting a role for the TRAPPII complex in tethering preciliary vesicles to the mother centriole during ciliogenesis. In summary, our findings have revealed an uncharacterized TRAPPII-specific component, C7orf43/TRAPPC14, that regulates preciliary trafficking of RABIN8 and ciliogenesis andsupport previous findings that the TRAPPII complex functions as a membrane tether.
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