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Nemitin, a Novel Map8/Map1s Interacting Protein with Wd40 Repeats (Nemitin Binds to MT via MAP8)

In neurons, a highly regulated microtubule cytoskeleton is essential for many cellular functions. These include axonal transport, regional specialization and synaptic function. Given the critical roles of microtubule-associated proteins (MAPs) in maintaining and regulating microtubule stability and... Full description

Journal Title: PLoS ONE 2012, Vol.7(4), p.e33094
Main Author: Wang, Wei
Other Authors: Lundin, Victor F , Millan, Ivan , Zeng, Anne , Chen, Xinyu , Yang, Jie , Allen, Elizabeth , Chen, Ningna , Bach, Gillian , Hsu, Andrew , Maloney, Michael T , Kapur, Mridu , Yang, Yanmin
Format: Electronic Article Electronic Article
Language: English
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ID: E-ISSN: 1932-6203 ; DOI: 10.1371/journal.pone.0033094
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recordid: plos10.1371/journal.pone.0033094
title: Nemitin, a Novel Map8/Map1s Interacting Protein with Wd40 Repeats (Nemitin Binds to MT via MAP8)
format: Article
creator:
  • Wang, Wei
  • Lundin, Victor F
  • Millan, Ivan
  • Zeng, Anne
  • Chen, Xinyu
  • Yang, Jie
  • Allen, Elizabeth
  • Chen, Ningna
  • Bach, Gillian
  • Hsu, Andrew
  • Maloney, Michael T
  • Kapur, Mridu
  • Yang, Yanmin
subjects:
  • Research Article
  • Biology
  • Genetics And Genomics
  • Cell Biology
  • Neuroscience
  • Biochemistry
ispartof: PLoS ONE, 2012, Vol.7(4), p.e33094
description: In neurons, a highly regulated microtubule cytoskeleton is essential for many cellular functions. These include axonal transport, regional specialization and synaptic function. Given the critical roles of microtubule-associated proteins (MAPs) in maintaining and regulating microtubule stability and dynamics, we sought to understand how this regulation is achieved. Here, we identify a novel LisH/WD40 repeat protein, tentatively named nemitin ( n euronal e nriched M AP i nteracting protein), as a potential regulator of MAP8-associated microtubule function. Based on expression at both the mRNA and protein levels, nemitin is enriched in the nervous system. Its protein expression is detected as early as embryonic day 11 and continues through adulthood. Interestingly, when expressed in non-neuronal cells, nemitin displays a diffuse pattern with puncta, although at the ultrastructural level it localizes along the microtubule network in vivo in sciatic nerves. These results suggest that the association of nemitin to microtubules may require an intermediary protein. Indeed, co-expression of nemitin with microtubule-associated protein 8 (MAP8) results in nemitin losing its diffuse pattern, instead decorating microtubules uniformly along with MAP8. Together, these results imply that nemitin may play an important role in regulating the neuronal cytoskeleton through an interaction with MAP8.
language: eng
source:
identifier: E-ISSN: 1932-6203 ; DOI: 10.1371/journal.pone.0033094
fulltext: fulltext
issn:
  • 1932-6203
  • 19326203
url: Link


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titleNemitin, a Novel Map8/Map1s Interacting Protein with Wd40 Repeats (Nemitin Binds to MT via MAP8)
creatorWang, Wei ; Lundin, Victor F ; Millan, Ivan ; Zeng, Anne ; Chen, Xinyu ; Yang, Jie ; Allen, Elizabeth ; Chen, Ningna ; Bach, Gillian ; Hsu, Andrew ; Maloney, Michael T ; Kapur, Mridu ; Yang, Yanmin
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identifierE-ISSN: 1932-6203 ; DOI: 10.1371/journal.pone.0033094
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descriptionIn neurons, a highly regulated microtubule cytoskeleton is essential for many cellular functions. These include axonal transport, regional specialization and synaptic function. Given the critical roles of microtubule-associated proteins (MAPs) in maintaining and regulating microtubule stability and dynamics, we sought to understand how this regulation is achieved. Here, we identify a novel LisH/WD40 repeat protein, tentatively named nemitin ( n euronal e nriched M AP i nteracting protein), as a potential regulator of MAP8-associated microtubule function. Based on expression at both the mRNA and protein levels, nemitin is enriched in the nervous system. Its protein expression is detected as early as embryonic day 11 and continues through adulthood. Interestingly, when expressed in non-neuronal cells, nemitin displays a diffuse pattern with puncta, although at the ultrastructural level it localizes along the microtubule network in vivo in sciatic nerves. These results suggest that the association of nemitin to microtubules may require an intermediary protein. Indeed, co-expression of nemitin with microtubule-associated protein 8 (MAP8) results in nemitin losing its diffuse pattern, instead decorating microtubules uniformly along with MAP8. Together, these results imply that nemitin may play an important role in regulating the neuronal cytoskeleton through an interaction with MAP8.
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titleNemitin, a Novel Map8/Map1s Interacting Protein with Wd40 Repeats (Nemitin Binds to MT via MAP8)
descriptionIn neurons, a highly regulated microtubule cytoskeleton is essential for many cellular functions. These include axonal transport, regional specialization and synaptic function. Given the critical roles of microtubule-associated proteins (MAPs) in maintaining and regulating microtubule stability and dynamics, we sought to understand how this regulation is achieved. Here, we identify a novel LisH/WD40 repeat protein, tentatively named nemitin ( n euronal e nriched M AP i nteracting protein), as a potential regulator of MAP8-associated microtubule function. Based on expression at both the mRNA and protein levels, nemitin is enriched in the nervous system. Its protein expression is detected as early as embryonic day 11 and continues through adulthood. Interestingly, when expressed in non-neuronal cells, nemitin displays a diffuse pattern with puncta, although at the ultrastructural level it localizes along the microtubule network in vivo in sciatic nerves. These results suggest that the association of nemitin to microtubules may require an intermediary protein. Indeed, co-expression of nemitin with microtubule-associated protein 8 (MAP8) results in nemitin losing its diffuse pattern, instead decorating microtubules uniformly along with MAP8. Together, these results imply that nemitin may play an important role in regulating the neuronal cytoskeleton through an interaction with MAP8.
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abstractIn neurons, a highly regulated microtubule cytoskeleton is essential for many cellular functions. These include axonal transport, regional specialization and synaptic function. Given the critical roles of microtubule-associated proteins (MAPs) in maintaining and regulating microtubule stability and dynamics, we sought to understand how this regulation is achieved. Here, we identify a novel LisH/WD40 repeat protein, tentatively named nemitin ( n euronal e nriched M AP i nteracting protein), as a potential regulator of MAP8-associated microtubule function. Based on expression at both the mRNA and protein levels, nemitin is enriched in the nervous system. Its protein expression is detected as early as embryonic day 11 and continues through adulthood. Interestingly, when expressed in non-neuronal cells, nemitin displays a diffuse pattern with puncta, although at the ultrastructural level it localizes along the microtubule network in vivo in sciatic nerves. These results suggest that the association of nemitin to microtubules may require an intermediary protein. Indeed, co-expression of nemitin with microtubule-associated protein 8 (MAP8) results in nemitin losing its diffuse pattern, instead decorating microtubules uniformly along with MAP8. Together, these results imply that nemitin may play an important role in regulating the neuronal cytoskeleton through an interaction with MAP8.
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