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Title: Spitzenkörper assembly mechanisms reveal conserved features of fungal and metazoan polarity scaffolds
Authors: Zheng, P.
Nguyen, T.A.
Wong, J.Y.
Lee, M.
Nguyen, T.-A. 
Fan, J.-S. 
Yang, D. 
Jedd, G. 
Issue Date: 5-Jun-2020
Publisher: Nature Research
Citation: Zheng, P., Nguyen, T.A., Wong, J.Y., Lee, M., Nguyen, T.-A., Fan, J.-S., Yang, D., Jedd, G. (2020-06-05). Spitzenkörper assembly mechanisms reveal conserved features of fungal and metazoan polarity scaffolds. Nature Communications 11 (1) : 2830. ScholarBank@NUS Repository.
Rights: Attribution 4.0 International
Abstract: The Spitzenkörper (SPK) constitutes a collection of secretory vesicles and polarity-related proteins intimately associated with polarized growth of fungal hyphae. Many SPK-localized proteins are known, but their assembly and dynamics remain poorly understood. Here, we identify protein-protein interaction cascades leading to assembly of two SPK scaffolds and recruitment of diverse effectors in Neurospora crassa. Both scaffolds are transported to the SPK by the myosin V motor (MYO-5), with the coiled-coil protein SPZ-1 acting as cargo adaptor. Neither scaffold appears to be required for accumulation of SPK secretory vesicles. One scaffold consists of Leashin-2 (LAH-2), which is required for SPK localization of the signalling kinase COT-1 and the glycolysis enzyme GPI-1. The other scaffold comprises a complex of Janus-1 (JNS-1) and the polarisome protein SPA-2. Via its Spa homology domain (SHD), SPA-2 recruits a calponin domain-containing F-actin effector (CCP-1). The SHD NMR structure reveals a conserved surface groove required for effector binding. Similarities between SPA-2/JNS-1 and the metazoan GIT/PIX complex identify foundational features of the cell polarity apparatus that predate the fungal-metazoan divergence. © 2020, The Author(s).
Source Title: Nature Communications
ISSN: 20411723
DOI: 10.1038/s41467-020-16712-9
Rights: Attribution 4.0 International
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