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Structure paper

TitleStructure of the RZZ complex and molecular basis of its interaction with Spindly.
Journal, issue, pagesJ Cell Biol, Vol. 216, Issue 4, Page 961-981, Year 2017
Publish dateApr 3, 2017
AuthorsShyamal Mosalaganti / Jenny Keller / Anika Altenfeld / Michael Winzker / Pascaline Rombaut / Michael Saur / Arsen Petrovic / Annemarie Wehenkel / Sabine Wohlgemuth / Franziska Müller / Stefano Maffini / Tanja Bange / Franz Herzog / Herbert Waldmann / Stefan Raunser / Andrea Musacchio /
PubMed AbstractKinetochores are macromolecular assemblies that connect chromosomes to spindle microtubules (MTs) during mitosis. The metazoan-specific ≈800-kD ROD-Zwilch-ZW10 (RZZ) complex builds a fibrous corona ...Kinetochores are macromolecular assemblies that connect chromosomes to spindle microtubules (MTs) during mitosis. The metazoan-specific ≈800-kD ROD-Zwilch-ZW10 (RZZ) complex builds a fibrous corona that assembles on mitotic kinetochores before MT attachment to promote chromosome alignment and robust spindle assembly checkpoint signaling. In this study, we combine biochemical reconstitutions, single-particle electron cryomicroscopy, cross-linking mass spectrometry, and structural modeling to build a complete model of human RZZ. We find that RZZ is structurally related to self-assembling cytosolic coat scaffolds that mediate membrane cargo trafficking, including Clathrin, Sec13-Sec31, and αβ'ε-COP. We show that Spindly, a dynein adaptor, is related to BicD2 and binds RZZ directly in a farnesylation-dependent but membrane-independent manner. Through a targeted chemical biology approach, we identify ROD as the Spindly farnesyl receptor. Our results suggest that RZZ is dynein's cargo at human kinetochores.
External linksJ Cell Biol / PubMed:28320825 / PubMed Central
MethodsEM (single particle)
Resolution10.4 - 26.0 Å
Structure data

EMDB-4103:
Structure of the human Rod-Zw10-Zwilch (RZZ) complex
Method: EM (single particle) / Resolution: 10.4 Å

EMDB-4104:
Negative stain reconstruction of the ROD(1-1250):Zwilch:ZW10
Method: EM (single particle) / Resolution: 26.0 Å

Source
  • Homo sapiens (human)

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