Tubulin Polymerization Promoting Protein, Ringmaker, and MAP1B Homolog Futsch Coordinate Microtubule Organization and Synaptic Growth
Ringmaker (Ringer) is homologous to the human Tubulin Polymerization Promoting Proteins (TPPPs) that are implicated in the stabilization and bundling of microtubules (MTs) that are particularly important for neurons and are also implicated in synaptic organization and plasticity. No functional data...
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Published in | Frontiers in cellular neuroscience Vol. 13; p. 192 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
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15.05.2019
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Abstract | Ringmaker (Ringer) is homologous to the human Tubulin Polymerization Promoting Proteins (TPPPs) that are implicated in the stabilization and bundling of microtubules (MTs) that are particularly important for neurons and are also implicated in synaptic organization and plasticity. No
functional data exist that have addressed the role of TPPP in synapse organization in any system. Here, we present the phenotypic and functional characterization of
mutants during
larval neuromuscular junction (NMJ) synaptic development.
mutants show reduced synaptic growth and transmission and display phenotypic similarities and genetic interactions with the
homolog of vertebrate Microtubule Associated Protein (MAP)1B,
Immunohistochemical and biochemical analyses show that individual and combined loss of Ringer and Futsch cause a significant reduction in MT loops at the NMJs and reduced acetylated-tubulin levels. Presynaptic over-expression of Ringer and Futsch causes elevated levels of acetylated-tubulin and significant increase in NMJ MT loops. These results indicate that Ringer and Futsch regulate synaptic MT organization in addition to synaptic growth. Together our findings may inform studies on the close mammalian homolog, TPPP, and provide insights into the role of MTs and associated proteins in synapse growth and organization. |
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AbstractList | Drosophila
Ringmaker (Ringer) is homologous to the human
T
ubulin
P
olymerization
P
romoting
P
roteins (TPPPs) that are implicated in the stabilization and bundling of microtubules (MTs) that are particularly important for neurons and are also implicated in synaptic organization and plasticity. No
in vivo
functional data exist that have addressed the role of TPPP in synapse organization in any system. Here, we present the phenotypic and functional characterization of
ringer
mutants during
Drosophila
larval neuromuscular junction (NMJ) synaptic development.
ringer
mutants show reduced synaptic growth and transmission and display phenotypic similarities and genetic interactions with the
Drosophila
homolog of vertebrate
M
icrotubule
A
ssociated
P
rotein (MAP)1B,
futsch.
Immunohistochemical and biochemical analyses show that individual and combined loss of Ringer and Futsch cause a significant reduction in MT loops at the NMJs and reduced acetylated-tubulin levels. Presynaptic over-expression of Ringer and Futsch causes elevated levels of acetylated-tubulin and significant increase in NMJ MT loops. These results indicate that Ringer and Futsch regulate synaptic MT organization in addition to synaptic growth. Together our findings may inform studies on the close mammalian homolog, TPPP, and provide insights into the role of MTs and associated proteins in synapse growth and organization. Drosophila Ringmaker (Ringer) is homologous to the human Tubulin Polymerization Promoting Proteins (TPPPs) that are implicated in the stabilization and bundling of microtubules (MTs) that are particularly important for neurons and are also implicated in synaptic organization and plasticity. No in vivo functional data exist that have addressed the role of TPPP in synapse organization in any system. Here, we present the phenotypic and functional characterization of ringer mutants during Drosophila larval neuromuscular junction (NMJ) synaptic development. ringer mutants show reduced synaptic growth and transmission and display phenotypic similarities and genetic interactions with the Drosophila homolog of vertebrate Microtubule Associated Protein (MAP)1B, futsch. Immunohistochemical and biochemical analyses show that individual and combined loss of Ringer and Futsch cause a significant reduction in MT loops at the NMJs and reduced acetylated-tubulin levels. Presynaptic over-expression of Ringer and Futsch causes elevated levels of acetylated-tubulin and significant increase in NMJ MT loops. These results indicate that Ringer and Futsch regulate synaptic MT organization in addition to synaptic growth. Together our findings may inform studies on the close mammalian homolog, TPPP, and provide insights into the role of MTs and associated proteins in synapse growth and organization. Ringmaker (Ringer) is homologous to the human Tubulin Polymerization Promoting Proteins (TPPPs) that are implicated in the stabilization and bundling of microtubules (MTs) that are particularly important for neurons and are also implicated in synaptic organization and plasticity. No functional data exist that have addressed the role of TPPP in synapse organization in any system. Here, we present the phenotypic and functional characterization of mutants during larval neuromuscular junction (NMJ) synaptic development. mutants show reduced synaptic growth and transmission and display phenotypic similarities and genetic interactions with the homolog of vertebrate Microtubule Associated Protein (MAP)1B, Immunohistochemical and biochemical analyses show that individual and combined loss of Ringer and Futsch cause a significant reduction in MT loops at the NMJs and reduced acetylated-tubulin levels. Presynaptic over-expression of Ringer and Futsch causes elevated levels of acetylated-tubulin and significant increase in NMJ MT loops. These results indicate that Ringer and Futsch regulate synaptic MT organization in addition to synaptic growth. Together our findings may inform studies on the close mammalian homolog, TPPP, and provide insights into the role of MTs and associated proteins in synapse growth and organization. |
Author | Neely, G Gregory Xie, Jing Shi, Qian Banerjee, Swati Saliba, Afaf Lin, Yong Qi |
AuthorAffiliation | 2 The Dr. John and Anne Chong Lab for Functional Genomics, Charles Perkins Centre and School of Life and Environmental Sciences, The University of Sydney , Sydney, NSW , Australia 1 Department of Cellular and Integrative Physiology, Long School of Medicine, University of Texas Health , San Antonio, TX , United States 3 Xiangya School of Medicine, Central South University , Changsha , China |
AuthorAffiliation_xml | – name: 3 Xiangya School of Medicine, Central South University , Changsha , China – name: 2 The Dr. John and Anne Chong Lab for Functional Genomics, Charles Perkins Centre and School of Life and Environmental Sciences, The University of Sydney , Sydney, NSW , Australia – name: 1 Department of Cellular and Integrative Physiology, Long School of Medicine, University of Texas Health , San Antonio, TX , United States |
Author_xml | – sequence: 1 givenname: Qian surname: Shi fullname: Shi, Qian organization: Department of Cellular and Integrative Physiology, Long School of Medicine, University of Texas Health, San Antonio, TX, United States – sequence: 2 givenname: Yong Qi surname: Lin fullname: Lin, Yong Qi organization: The Dr. John and Anne Chong Lab for Functional Genomics, Charles Perkins Centre and School of Life and Environmental Sciences, The University of Sydney, Sydney, NSW, Australia – sequence: 3 givenname: Afaf surname: Saliba fullname: Saliba, Afaf organization: Department of Cellular and Integrative Physiology, Long School of Medicine, University of Texas Health, San Antonio, TX, United States – sequence: 4 givenname: Jing surname: Xie fullname: Xie, Jing organization: Xiangya School of Medicine, Central South University, Changsha, China – sequence: 5 givenname: G Gregory surname: Neely fullname: Neely, G Gregory organization: The Dr. John and Anne Chong Lab for Functional Genomics, Charles Perkins Centre and School of Life and Environmental Sciences, The University of Sydney, Sydney, NSW, Australia – sequence: 6 givenname: Swati surname: Banerjee fullname: Banerjee, Swati organization: Department of Cellular and Integrative Physiology, Long School of Medicine, University of Texas Health, San Antonio, TX, United States |
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Keywords | acetylation microtubule Ringmaker Futsch TPPP synapse |
Language | English |
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Notes | Edited by: Davide Cervia, Università degli Studi della Tuscia, Italy This article was submitted to Cellular Neurophysiology, a section of the journal Frontiers in Cellular Neuroscience Reviewed by: Timothy Mosca, Thomas Jefferson University, United States; Archan Ganguly, University of California, San Diego, United States; Judit Ovadi, Hungarian Academy of Sciences (MTA), Hungary |
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Snippet | Ringmaker (Ringer) is homologous to the human Tubulin Polymerization Promoting Proteins (TPPPs) that are implicated in the stabilization and bundling of... Drosophila Ringmaker (Ringer) is homologous to the human Tubulin Polymerization Promoting Proteins (TPPPs) that are implicated in the stabilization and... Drosophila Ringmaker (Ringer) is homologous to the human T ubulin P olymerization P romoting P roteins (TPPPs) that are implicated in the stabilization and... |
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SubjectTerms | acetylation Cytoskeleton Drosophila Functional plasticity Futsch Insects microtubule Microtubule-associated protein 1 Microtubules Nervous system Neuromuscular junctions Neuroscience Overexpression Polymerization Proteins Ringmaker synapse Synaptic plasticity Synaptic transmission Synaptogenesis TPPP Tubulin |
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Title | Tubulin Polymerization Promoting Protein, Ringmaker, and MAP1B Homolog Futsch Coordinate Microtubule Organization and Synaptic Growth |
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