IC138 defines a subdomain at the base of the I1 dynein that regulates microtubule sliding and flagellar motility

Raqual Bower, Kristyn VanderWaal, Eileen O'Toole, Laura Fox, Catherine Perrone, Joshua Mueller, Maureen Wirschell, R. Kamiya, Winfield S. Sale, Mary E. Porter

Research output: Contribution to journalArticle

44 Citations (Scopus)

Abstract

To understand the mechanisms that regulate the assembly and activity of flagellar dyneins, we focused on the I1 inner arm dynein (dynein f) and a null allele, bop5-2, defective in the gene encoding the IC138 phosphoprotein subunit. I1 dynein assembles in bop5-2 axonemes but lacks at least four subunits: IC138, IC97, LC7b, and flagellar-associated protein (FAP) 120 - defining a new I1 subcomplex. Electron microscopy and image averaging revealed a defect at the base of the I1 dynein, in between radial spoke 1 and the outer dynein arms. Microtubule sliding velocities also are reduced. Transformation with wild-type IC138 restores assembly of the IC138 subcomplex and rescues microtubule sliding. These observations suggest that the IC138 subcomplex is required to coordinate I1 motor activity. To further test this hypothesis, we analyzed microtubule sliding in radial spoke and double mutant strains. The results reveal an essential role for the IC138 subcomplex in the regulation of I1 activity by the radial spoke/phosphorylation pathway.

Original languageEnglish (US)
Pages (from-to)3055-3063
Number of pages9
JournalMolecular biology of the cell
Volume20
Issue number13
DOIs
StatePublished - Jul 1 2009

Fingerprint

Dyneins
Microtubules
Axoneme
Phosphoproteins
Electron Microscopy
Motor Activity
Alleles
Phosphorylation
Genes
Proteins

Cite this

IC138 defines a subdomain at the base of the I1 dynein that regulates microtubule sliding and flagellar motility. / Bower, Raqual; VanderWaal, Kristyn; O'Toole, Eileen; Fox, Laura; Perrone, Catherine; Mueller, Joshua; Wirschell, Maureen; Kamiya, R.; Sale, Winfield S.; Porter, Mary E.

In: Molecular biology of the cell, Vol. 20, No. 13, 01.07.2009, p. 3055-3063.

Research output: Contribution to journalArticle

Bower, R, VanderWaal, K, O'Toole, E, Fox, L, Perrone, C, Mueller, J, Wirschell, M, Kamiya, R, Sale, WS & Porter, ME 2009, 'IC138 defines a subdomain at the base of the I1 dynein that regulates microtubule sliding and flagellar motility', Molecular biology of the cell, vol. 20, no. 13, pp. 3055-3063. https://doi.org/10.1091/mbc.E09-04-0277
Bower, Raqual ; VanderWaal, Kristyn ; O'Toole, Eileen ; Fox, Laura ; Perrone, Catherine ; Mueller, Joshua ; Wirschell, Maureen ; Kamiya, R. ; Sale, Winfield S. ; Porter, Mary E. / IC138 defines a subdomain at the base of the I1 dynein that regulates microtubule sliding and flagellar motility. In: Molecular biology of the cell. 2009 ; Vol. 20, No. 13. pp. 3055-3063.
@article{d682cd4f70584a4bb61b4fa1deed04fe,
title = "IC138 defines a subdomain at the base of the I1 dynein that regulates microtubule sliding and flagellar motility",
abstract = "To understand the mechanisms that regulate the assembly and activity of flagellar dyneins, we focused on the I1 inner arm dynein (dynein f) and a null allele, bop5-2, defective in the gene encoding the IC138 phosphoprotein subunit. I1 dynein assembles in bop5-2 axonemes but lacks at least four subunits: IC138, IC97, LC7b, and flagellar-associated protein (FAP) 120 - defining a new I1 subcomplex. Electron microscopy and image averaging revealed a defect at the base of the I1 dynein, in between radial spoke 1 and the outer dynein arms. Microtubule sliding velocities also are reduced. Transformation with wild-type IC138 restores assembly of the IC138 subcomplex and rescues microtubule sliding. These observations suggest that the IC138 subcomplex is required to coordinate I1 motor activity. To further test this hypothesis, we analyzed microtubule sliding in radial spoke and double mutant strains. The results reveal an essential role for the IC138 subcomplex in the regulation of I1 activity by the radial spoke/phosphorylation pathway.",
author = "Raqual Bower and Kristyn VanderWaal and Eileen O'Toole and Laura Fox and Catherine Perrone and Joshua Mueller and Maureen Wirschell and R. Kamiya and Sale, {Winfield S.} and Porter, {Mary E.}",
year = "2009",
month = "7",
day = "1",
doi = "10.1091/mbc.E09-04-0277",
language = "English (US)",
volume = "20",
pages = "3055--3063",
journal = "Molecular Biology of the Cell",
issn = "1059-1524",
publisher = "American Society for Cell Biology",
number = "13",

}

TY - JOUR

T1 - IC138 defines a subdomain at the base of the I1 dynein that regulates microtubule sliding and flagellar motility

AU - Bower, Raqual

AU - VanderWaal, Kristyn

AU - O'Toole, Eileen

AU - Fox, Laura

AU - Perrone, Catherine

AU - Mueller, Joshua

AU - Wirschell, Maureen

AU - Kamiya, R.

AU - Sale, Winfield S.

AU - Porter, Mary E.

PY - 2009/7/1

Y1 - 2009/7/1

N2 - To understand the mechanisms that regulate the assembly and activity of flagellar dyneins, we focused on the I1 inner arm dynein (dynein f) and a null allele, bop5-2, defective in the gene encoding the IC138 phosphoprotein subunit. I1 dynein assembles in bop5-2 axonemes but lacks at least four subunits: IC138, IC97, LC7b, and flagellar-associated protein (FAP) 120 - defining a new I1 subcomplex. Electron microscopy and image averaging revealed a defect at the base of the I1 dynein, in between radial spoke 1 and the outer dynein arms. Microtubule sliding velocities also are reduced. Transformation with wild-type IC138 restores assembly of the IC138 subcomplex and rescues microtubule sliding. These observations suggest that the IC138 subcomplex is required to coordinate I1 motor activity. To further test this hypothesis, we analyzed microtubule sliding in radial spoke and double mutant strains. The results reveal an essential role for the IC138 subcomplex in the regulation of I1 activity by the radial spoke/phosphorylation pathway.

AB - To understand the mechanisms that regulate the assembly and activity of flagellar dyneins, we focused on the I1 inner arm dynein (dynein f) and a null allele, bop5-2, defective in the gene encoding the IC138 phosphoprotein subunit. I1 dynein assembles in bop5-2 axonemes but lacks at least four subunits: IC138, IC97, LC7b, and flagellar-associated protein (FAP) 120 - defining a new I1 subcomplex. Electron microscopy and image averaging revealed a defect at the base of the I1 dynein, in between radial spoke 1 and the outer dynein arms. Microtubule sliding velocities also are reduced. Transformation with wild-type IC138 restores assembly of the IC138 subcomplex and rescues microtubule sliding. These observations suggest that the IC138 subcomplex is required to coordinate I1 motor activity. To further test this hypothesis, we analyzed microtubule sliding in radial spoke and double mutant strains. The results reveal an essential role for the IC138 subcomplex in the regulation of I1 activity by the radial spoke/phosphorylation pathway.

UR - http://www.scopus.com/inward/record.url?scp=67650427411&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=67650427411&partnerID=8YFLogxK

U2 - 10.1091/mbc.E09-04-0277

DO - 10.1091/mbc.E09-04-0277

M3 - Article

C2 - 19420135

AN - SCOPUS:67650427411

VL - 20

SP - 3055

EP - 3063

JO - Molecular Biology of the Cell

JF - Molecular Biology of the Cell

SN - 1059-1524

IS - 13

ER -