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Your search keyword '"Mathias, Wittau"' showing total 2 results
Start Over Author "Mathias, Wittau" Journal biochimica et biophysica acta (bba) - molecular cell research
2 results on '"Mathias, Wittau"'

1. Corrigendum to 'interaction of casein kinase 1 delta (CK1 < delta >) with the light chain LC2 of microtubule associated protein 1A (MAP1A)' [Biochim. Biophys. Acta 1745/2 (2005) 196–2006]

Author

Zhenyu Xiao, Sonja Wolff, Mathias Wittau, Nadine Süssner, Martin Stöter, and Uwe Knippschild

Subjects
Casein Kinase 1 delta, Biochemistry, Chemistry, Microtubule associated protein 1A, Cell Biology, Casein kinase 1, Immunoglobulin light chain, Molecular Biology
Published
2017
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2. Interaction of casein kinase 1 delta (CK1δ) with the light chain LC2 of microtubule associated protein 1A (MAP1A)

Author

Zhenyu Xiao, Martin Stöter, Nadine Süssner, Uwe Knippschild, Mathias Wittau, and Sonja Wolff

Subjects
Molecular Sequence Data, Microtubule, MAP1A, Biology, Immunoglobulin light chain, Cell Line, Serine, Yeast two-hybrid screen, Two-Hybrid System Techniques, Animals, Threonine, Phosphorylation, Molecular Biology, Base Sequence, Kinase, CK1δ, Cell Biology, Rats, Casein Kinase 1 delta, Isoenzymes, Protein Subunits, Biochemistry, Casein Kinase Idelta, Mutation, Casein kinase 1, Microtubule-Associated Proteins
Abstract

CK1delta, a member of the casein kinase 1 family of serine/threonine specific kinases, has been shown to be involved in the regulation of microtubule dynamics. We have now identified a 176 aa fragment of the light chain LC2 of MAP1A (termed LC2-P16) specifically interacting with CK1delta. Two CK1delta interacting domains of LC2 were identified, located between aa 2629 and 2753 close to aa 2683 and between aa 2712 and 2805 of LC2. The two regions necessary for the interaction of LC2 with CK1delta have been mapped between aa 76-103 and aa 351-375 of CK1delta. Furthermore, LC2 has been identified as a new substrate of CK1delta. We therefore propose a model in which CK1delta could modulate microtubule dynamics by changing the phosphorylation status of the light chain LC2 of MAP1A.

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