date: 2019-03-16T08:25:47Z
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pdf:docinfo:title: Structure and Functions of Microtubule Associated Proteins Tau and MAP2c: Similarities and Differences
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subject: The stability and dynamics of cytoskeleton in brain nerve cells are regulated by microtubule associated proteins (MAPs), tau and MAP2. Both proteins are intrinsically disordered and involved in multiple molecular interactions important for normal physiology and pathology of chronic neurodegenerative diseases. Nuclear magnetic resonance and cryo-electron microscopy recently revealed propensities of MAPs to form transient local structures and long-range contacts in the free state, and conformations adopted in complexes with microtubules and filamentous actin, as well as in pathological aggregates. In this paper, we compare the longest, 441-residue brain isoform of tau (tau40), and a 467-residue isoform of MAP2, known as MAP2c. For both molecules, we present transient structural motifs revealed by conformational analysis of experimental data obtained for free soluble forms of the proteins. We show that many of the short sequence motifs that exhibit transient structural features are linked to functional properties, manifested by specific interactions. The transient structural motifs can be therefore classified as molecular recognition elements of tau40 and MAP2c. Their interactions are further regulated by post-translational modifications, in particular phosphorylation. The structure-function analysis also explains differences between biological activities of tau40 and MAP2c.
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dc:title: Structure and Functions of Microtubule Associated Proteins Tau and MAP2c: Similarities and Differences
modified: 2019-03-16T08:25:47Z
cp:subject: The stability and dynamics of cytoskeleton in brain nerve cells are regulated by microtubule associated proteins (MAPs), tau and MAP2. Both proteins are intrinsically disordered and involved in multiple molecular interactions important for normal physiology and pathology of chronic neurodegenerative diseases. Nuclear magnetic resonance and cryo-electron microscopy recently revealed propensities of MAPs to form transient local structures and long-range contacts in the free state, and conformations adopted in complexes with microtubules and filamentous actin, as well as in pathological aggregates. In this paper, we compare the longest, 441-residue brain isoform of tau (tau40), and a 467-residue isoform of MAP2, known as MAP2c. For both molecules, we present transient structural motifs revealed by conformational analysis of experimental data obtained for free soluble forms of the proteins. We show that many of the short sequence motifs that exhibit transient structural features are linked to functional properties, manifested by specific interactions. The transient structural motifs can be therefore classified as molecular recognition elements of tau40 and MAP2c. Their interactions are further regulated by post-translational modifications, in particular phosphorylation. The structure-function analysis also explains differences between biological activities of tau40 and MAP2c.
pdf:docinfo:subject: The stability and dynamics of cytoskeleton in brain nerve cells are regulated by microtubule associated proteins (MAPs), tau and MAP2. Both proteins are intrinsically disordered and involved in multiple molecular interactions important for normal physiology and pathology of chronic neurodegenerative diseases. Nuclear magnetic resonance and cryo-electron microscopy recently revealed propensities of MAPs to form transient local structures and long-range contacts in the free state, and conformations adopted in complexes with microtubules and filamentous actin, as well as in pathological aggregates. In this paper, we compare the longest, 441-residue brain isoform of tau (tau40), and a 467-residue isoform of MAP2, known as MAP2c. For both molecules, we present transient structural motifs revealed by conformational analysis of experimental data obtained for free soluble forms of the proteins. We show that many of the short sequence motifs that exhibit transient structural features are linked to functional properties, manifested by specific interactions. The transient structural motifs can be therefore classified as molecular recognition elements of tau40 and MAP2c. Their interactions are further regulated by post-translational modifications, in particular phosphorylation. The structure-function analysis also explains differences between biological activities of tau40 and MAP2c.
pdf:docinfo:creator: Kate?ina Melková, Vojt?ch Zapletal, Subhash Narasimhan, Séverine Jansen, Jozef Hritz, Rostislav ?krabana, Markus Zweckstetter, Malene Ringkjřbing Jensen, Martin Blackledge and Luká? ?ídek
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meta:author: Kate?ina Melková, Vojt?ch Zapletal, Subhash Narasimhan, Séverine Jansen, Jozef Hritz, Rostislav ?krabana, Markus Zweckstetter, Malene Ringkjřbing Jensen, Martin Blackledge and Luká? ?ídek
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Author: Kate?ina Melková, Vojt?ch Zapletal, Subhash Narasimhan, Séverine Jansen, Jozef Hritz, Rostislav ?krabana, Markus Zweckstetter, Malene Ringkjřbing Jensen, Martin Blackledge and Luká? ?ídek
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Keywords: microtubule associated protein; tau; intrinsically disordered protein; phosphorylation; nuclear magnetic resonance
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dc:creator: Kate?ina Melková, Vojt?ch Zapletal, Subhash Narasimhan, Séverine Jansen, Jozef Hritz, Rostislav ?krabana, Markus Zweckstetter, Malene Ringkjřbing Jensen, Martin Blackledge and Luká? ?ídek
dcterms:created: 2019-03-16T08:25:47Z
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title: Structure and Functions of Microtubule Associated Proteins Tau and MAP2c: Similarities and Differences
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pdf:docinfo:keywords: microtubule associated protein; tau; intrinsically disordered protein; phosphorylation; nuclear magnetic resonance
pdf:docinfo:modified: 2019-03-16T08:25:47Z
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creator: Kate?ina Melková, Vojt?ch Zapletal, Subhash Narasimhan, Séverine Jansen, Jozef Hritz, Rostislav ?krabana, Markus Zweckstetter, Malene Ringkjřbing Jensen, Martin Blackledge and Luká? ?ídek
dc:subject: microtubule associated protein; tau; intrinsically disordered protein; phosphorylation; nuclear magnetic resonance
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meta:keyword: microtubule associated protein; tau; intrinsically disordered protein; phosphorylation; nuclear magnetic resonance
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pdf:docinfo:created: 2019-03-16T08:25:47Z