Spitzenkörper assembly mechanisms reveal conserved features of fungal and metazoan polarity scaffolds

• Published in: Nature communications Vol. 11; no. 1; p. 2830
• Main Authors: Zheng, Peng, Nguyen, Tu Anh, Wong, Jie Yun, Lee, Michelle, Nguyen, The-Anh, Fan, Jing-Song, Yang, Daiwen, Jedd, Gregory
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 05.06.2020; Nature Publishing Group; Nature Portfolio
• Subjects: 14/19; 42/35; 631/326/193/2538; 631/326/88; 631/80/85; 82/58; 82/80; Accumulation; Actin; Analogies; Assembly; Calponin; Cell Polarity; Coils; Divergence; Domains; Fungal Proteins - chemistry; Fungal Proteins - metabolism; Fungi; Glycolysis; Grooves; Homology; Humanities and Social Sciences; Hyphae; Hyphae - cytology; Hyphae - metabolism; Kinases; Localization; multidisciplinary; Myosin; Myosin Type V - chemistry; Myosin Type V - metabolism; Neurospora; Neurospora crassa - cytology; Neurospora crassa - metabolism; NMR; Nuclear magnetic resonance; Nuclear Magnetic Resonance, Biomolecular; Polarity; Protein Domains; Protein interaction; Protein Interaction Maps; Proteins; Scaffolds; Science; Science (multidisciplinary); Secretory vesicles; Secretory Vesicles - metabolism; Vesicles

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 intera...