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Abstract Detail



Evolution of Hyphal Function and Development

Lara-Rojas, F. [1], Bartnicki-Garcia, S. [1], Mouriño-Pérez, Rosa R. [1].

Proteins involved in early stages of endocytosis in Neurospora crassa.

Actin is a key component for the establishment and maintenance of the polarized apical growth characteristic of hyphal cells. In Neurospora crassa, F-actin is present throughout the hyphal cytoplasm including the core of Spitzenkörper, whereas actin patches together with several components of the endocytic machinery are found in the endocytic collar located in the sub-apical region. The proximity of these endocytic sites to the apex suggests that this process may be part of the machinery involved in apical growth. To investigate this possibility we used deletion mutants together with fluorescent-protein tagging to characterize three proteins known to play different molecular roles during endocytosis: the adaptor protein SLA-1 and two actin binding proteins, WASP (Wiskott - Aldrich syndrome Protein) and MYO-1 (myosin class I). The three deletion mutants showed marked but different reductions in growth rate, irregular branching, reduced aerial mycelia and poor or no conidiation. By visualizing actin with the Lifeact-GFP reporter, we found that the absence of myo-1 or sla1 alters the actin cytoskeleton, leading to periods of polarized and isotropic growth of the hyphae. MYO-1-GFP is located in the endocytic collar and also forms part of the actomyosin ring during septum formation as is true of other endocytic proteins. Our findings indicate the importance of endocytic proteins in the stability of the actin cytoskeleton and in maintaining normal hyphal morphogenesis.


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1 - Centro de Investigación y Educación Superior de Ensenada (CICESE), Departamento de Microbiología, Ensenada, Mexico

Keywords:
LifeAct-GFP
actomyosin ring.

Presentation Type: Symposium or Colloquium Presentation
Session: SY6
Location: Room 104 AB/Kellogg Hotel and Conference Center
Date: Tuesday, June 10th, 2014
Time: 1:30 PM
Number: SY6002
Abstract ID:214
Candidate for Awards:None


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