Interaction of MAP2c with SH3 domain of plectin

Erik Nomilner¹, Kateřina Melková^1,2, Vojtěch Zapletal^1,2, Séverine Jansen¹, Lukáš Žídek^1,2

¹Central European Institute of Technology, Masaryk University, Kamenice 5, CZ-625 00, Brno,
Czech Republic.

²National Centre for Biomolecular Research, Faculty of Science, Masaryk University, Kamenice 5, CZ-625 00, Brno, Czech Republic.

Microtubule associated protein 2c (MAP2c) is an intrinsically disordered protein (IDP) which belongs to a MAP2 subfamily expressed in the developing neurons and can be found mainly in their dendrites [1]. MAP2c binds to microtubules regulates their dynamics in a phosphorylation dependent manner, which is essential for the correct function of cytoskeleton of neural cells and its dysfunction may be one of the reasons of the development of neurodegenerative diseases [2]–[4].

Plectin, the cytolinker between three main cytoskeletal components (actin microfilaments, microtubules (MT) and intermediate filaments), act as an MT destabilizer [5]. Its SH3 domain seems to interact with several regions of MAP2c, which show interesting conformational behaviour.

In our work we used various NMR experiments in order to investigate the interaction between MAP2c and the SH3 domain of plectin and dynamic properties of the binding site. In order to understand the nature of this interaction we applied HNCO NMR experiments on full-length MAP2c and its shorter constructs to describe also the effect of absence of other functional domains to this interaction.

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[4]        B. Weissnarr, T. Doll, and A. Matus, “Reorganisation of the microtubular cytoskeleton by embryonic microtubule-associated protein 2 (MAP2c),” p. 11.

[5]        R. G. Valencia et al., “Intermediate filament-associated cytolinker plectin 1c destabilizes microtubules in keratinocytes,” Mol. Biol. Cell, vol. 24, no. 6, pp. 768–784, Mar. 2013.