Structural Basis for the Association of MAP6 Protein with Microtubules and Its Regulation by Calmodulin

Lefèvre, Julien; Savarin, Philippe; Gans, Pierre; Hamon, Loïc; Clément, Marie‐Jeanne; David, M; Bosc, Christophe; Andrieux, Annie; Curmi, Patrick A.

doi:10.1074/jbc.m113.457267

Cited by 26 publications

(28 citation statements)

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“…Calmodulin is also known to bind IP3 receptor and regulates its calcium channel activity (Kasri et al , 2006). It is intriguing that calmodulin has also been implicated in regulating microtubule dynamics via microtubule-associated proteins (Lefevre et al , 2013). …”

Section: Discussionmentioning

confidence: 99%

Spindle function inXenopusoocytes involves possible nanodomain calcium signaling

Leblanc

et al. 2016

MBoC

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Section: Discussionmentioning

confidence: 99%

Spindle function inXenopusoocytes involves possible nanodomain calcium signaling

Leblanc

et al. 2016

MBoC

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“…There are several proteins that interact with both the actin and microtubule cytoskeletons to enable cross talk between the two cytoskeletal networks (Bartolini and Gundersen, 2010). However, the interactions between MAP6 and microtubules or actin may be mutually exclusive and appear tightly regulated by phosphorylation (Baratier et al, 2006;Lefevre et al, 2013).…”

Section: Map6/stopmentioning

confidence: 99%

“…Many studies have focused on the phosphorylation of MAP6 by CaMKII (Bosc et al, 2001;Bosc et al, 2003;Baratier et al, 2006). MAP6 is phosphorylated by CaMKII in vitro on at least three of the four potential CaMKII consensus sites found within its sequence: Ser139, Ser198, and Ser491 (Baratier et al, 2006;Lefevre et al, 2013). Phosphorylation of MAP6 by CaMKII causes MAP6 to dissociate from the microtubule (Lefevre et al, 2013).…”

Section: Map6/stopmentioning

confidence: 99%

“…MAP6 is phosphorylated by CaMKII in vitro on at least three of the four potential CaMKII consensus sites found within its sequence: Ser139, Ser198, and Ser491 (Baratier et al, 2006;Lefevre et al, 2013). Phosphorylation of MAP6 by CaMKII causes MAP6 to dissociate from the microtubule (Lefevre et al, 2013). In vivo, phosphorylation is normally preceded by synaptic activation and causes a redistribution of MAP6 from primary branches to synaptic compartments (Baratier et al, 2006).…”

Section: Map6/stopmentioning

confidence: 99%

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ReMAPping the microtubule landscape: How phosphorylation dictates the activities of microtubule‐associated proteins

Ramkumar

Jong

Ori-McKenney

2017

Developmental Dynamics

156

111

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Classical microtubule-associated proteins (MAPs) were originally identified based on their co-purification with microtubules assembled from mammalian brain lysate. They have since been found to perform a range of functions involved in regulating the dynamics of the microtubule cytoskeleton. Most of these MAPs play integral roles in microtubule organization during neuronal development, microtubule remodeling during neuronal activity, and microtubule stabilization during neuronal maintenance. As a result, mutations in MAPs contribute to neurodevelopmental disorders, psychiatric conditions, and neurodegenerative diseases. MAPs are post-translationally regulated by phosphorylation depending on developmental time point and cellular context. Phosphorylation can affect the microtubule affinity, cellular localization, or overall function of a particular MAP and can thus have profound implications for neuronal health. Here we review MAP1, MAP2, MAP4, MAP6, MAP7, MAP9, tau, and DCX, and how each is regulated by phosphorylation in neuronal physiology and disease. Developmental Dynamics 247:138-155,

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“…Microtubule assembly is subsequently regulated by calcium-loaded calmodulin (Ca 2+ /CaM) via direct binding to MAPs (24)(25)(26). Calmodulin (CaM) is a relatively small calcium-binding protein involved in many signaling pathways that regulate a large number of crucial cellular processes (27).…”

Section: Peptidyl-prolyl Cis/trans Isomerase Parvulin 17 (Par17) Intementioning

confidence: 99%

Parvulin 17-catalyzed Tubulin Polymerization Is Regulated by Calmodulin in a Calcium-dependent Manner

Burgardt

Schmidt

Manns

et al. 2015

Journal of Biological Chemistry

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Recently we have shown that the peptidyl-prolyl cis/trans isomerase parvulin 17 (Par17) interacts with tubulin in a GTP-dependent manner, thereby promoting the formation of microtubules. Microtubule assembly is regulated by Ca(2+)-loaded calmodulin (Ca(2+)/CaM) both in the intact cell and under in vitro conditions via direct interaction with microtubule-associated proteins. Here we provide the first evidence that Ca(2+)/CaM interacts also with Par17 in a physiologically relevant way, thus preventing Par17-promoted microtubule assembly. In contrast, parvulin 14 (Par14), which lacks only the first 25 N-terminal residues of the Par17 sequence, does not interact with Ca(2+)/CaM, indicating that this interaction is exclusive for Par17. Pulldown experiments and chemical shift perturbation analysis with (15)N-labeled Par17 furthermore confirmed that calmodulin (CaM) interacts in a Ca(2+)-dependent manner with the Par17 N terminus. The reverse experiment with (15)N-labeled Ca(2+)/CaM demonstrated that the N-terminal Par17 segment binds to both CaM lobes simultaneously, indicating that Ca(2+)/CaM undergoes a conformational change to form a binding channel between its two lobes, apparently similar to the structure of the CaM-smMLCK(796-815) complex. In vitro tubulin polymerization assays furthermore showed that Ca(2+)/CaM completely suppresses Par17-promoted microtubule assembly. The results imply that Ca(2+)/CaM binding to the N-terminal segment of Par17 causes steric hindrance of the Par17 active site, thus interfering with the Par17/tubulin interaction. This Ca(2+)/CaM-mediated control of Par17-assisted microtubule assembly may provide a mechanism that couples Ca(2+) signaling with microtubule function.

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Structural Basis for the Association of MAP6 Protein with Microtubules and Its Regulation by Calmodulin

Cited by 26 publications

References 50 publications

Spindle function inXenopusoocytes involves possible nanodomain calcium signaling

Spindle function inXenopusoocytes involves possible nanodomain calcium signaling

ReMAPping the microtubule landscape: How phosphorylation dictates the activities of microtubule‐associated proteins

Parvulin 17-catalyzed Tubulin Polymerization Is Regulated by Calmodulin in a Calcium-dependent Manner

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