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Functionally distinct kinesin-13 family members cooperate to regulate microtubule dynamics during interphase

Functionally distinct kinesin-13 family members cooperate to regulate microtubule dynamics during interphase
Functionally distinct kinesin-13 family members cooperate to regulate microtubule dynamics during interphase

Regulation of microtubule polymerization and depolymerization is required for proper cell development. Here, we report that two proteins of the Drosophila melanogaster kinesin-13 family, KLP10A and KLP59C, cooperate to drive microtubule depolymerization in interphase cells. Analyses of microtubule dynamics in S2 cells depleted of these proteins indicate that both proteins stimulate depolymerization, but alter distinct parameters of dynamic instability; KLP10A stimulates catastrophe (a switch from growth to shrinkage) whereas KLP59C suppresses rescue (a switch from shrinkage to growth). Moreover, immunofluorescence and live analyses of cells expressing tagged kinesins reveal that KLP10A and KLP59C target to polymerizing and depolymerizing microtubule plus ends, respectively. Our data also suggest that KLP10A is deposited on microtubules by the plus-end tracking protein, EB1. Our findings support a model in which these two members of the kinesin-13 family divide the labour of microtubule depolymerization.

Animals, Blotting, Western, Cell Line, Drosophila, Drosophila melanogaster, Glutathione Transferase/metabolism, Green Fluorescent Proteins/metabolism, Interphase, Kinesin/chemistry, Microscopy, Fluorescence, Microtubules/ultrastructure, Models, Biological, Polymers/chemistry, Protein Structure, Tertiary, RNA Interference, RNA, Double-Stranded/chemistry, Time Factors
1465-7392
235-45
Mennella, Vito
43c60e29-c0a7-4ab8-8e5c-fcb59f70a28a
Rogers, Gregory C
191cb941-d7fe-4868-84bf-ecb8a2b56c3e
Rogers, Stephen L
85b2c656-4552-4820-bbef-67db4e2992f8
Buster, Daniel W
8618c713-96b5-4bda-bc32-88cc7a793b46
Vale, Ronald D
c429e3bc-6326-48e7-83ac-eb77d26373c1
Sharp, David J
0e701ea9-7d32-4884-a57c-51b927c76ba3
Mennella, Vito
43c60e29-c0a7-4ab8-8e5c-fcb59f70a28a
Rogers, Gregory C
191cb941-d7fe-4868-84bf-ecb8a2b56c3e
Rogers, Stephen L
85b2c656-4552-4820-bbef-67db4e2992f8
Buster, Daniel W
8618c713-96b5-4bda-bc32-88cc7a793b46
Vale, Ronald D
c429e3bc-6326-48e7-83ac-eb77d26373c1
Sharp, David J
0e701ea9-7d32-4884-a57c-51b927c76ba3

Mennella, Vito, Rogers, Gregory C, Rogers, Stephen L, Buster, Daniel W, Vale, Ronald D and Sharp, David J (2005) Functionally distinct kinesin-13 family members cooperate to regulate microtubule dynamics during interphase. Nature Cell Biology, 7 (3), 235-45. (doi:10.1038/ncb1222).

Record type: Article

Abstract

Regulation of microtubule polymerization and depolymerization is required for proper cell development. Here, we report that two proteins of the Drosophila melanogaster kinesin-13 family, KLP10A and KLP59C, cooperate to drive microtubule depolymerization in interphase cells. Analyses of microtubule dynamics in S2 cells depleted of these proteins indicate that both proteins stimulate depolymerization, but alter distinct parameters of dynamic instability; KLP10A stimulates catastrophe (a switch from growth to shrinkage) whereas KLP59C suppresses rescue (a switch from shrinkage to growth). Moreover, immunofluorescence and live analyses of cells expressing tagged kinesins reveal that KLP10A and KLP59C target to polymerizing and depolymerizing microtubule plus ends, respectively. Our data also suggest that KLP10A is deposited on microtubules by the plus-end tracking protein, EB1. Our findings support a model in which these two members of the kinesin-13 family divide the labour of microtubule depolymerization.

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More information

e-pub ahead of print date: 20 February 2005
Published date: March 2005
Keywords: Animals, Blotting, Western, Cell Line, Drosophila, Drosophila melanogaster, Glutathione Transferase/metabolism, Green Fluorescent Proteins/metabolism, Interphase, Kinesin/chemistry, Microscopy, Fluorescence, Microtubules/ultrastructure, Models, Biological, Polymers/chemistry, Protein Structure, Tertiary, RNA Interference, RNA, Double-Stranded/chemistry, Time Factors

Identifiers

Local EPrints ID: 434093
URI: http://eprints.soton.ac.uk/id/eprint/434093
ISSN: 1465-7392
PURE UUID: 8e73a235-7fc8-48b7-a979-4dbb93bbb2c7
ORCID for Vito Mennella: ORCID iD orcid.org/0000-0002-4842-9012

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Date deposited: 12 Sep 2019 16:30
Last modified: 16 Mar 2024 04:04

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Contributors

Author: Vito Mennella ORCID iD
Author: Gregory C Rogers
Author: Stephen L Rogers
Author: Daniel W Buster
Author: Ronald D Vale
Author: David J Sharp

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