2P199 Conformational Changes of Inner-Arm Dynein f from Chlamydomonas Coupled with Phosphorylation of Its Intermediated Chain IC138. III(37. Molecular motor (II),Poster Session,Abstract,Meeting Program of EABS &amp; BSJ 2006)

Sakakibara, Hitoshi; Burgess, Stanley A; Sakai, Y.

doi:10.2142/biophys.46.s345_3

Cited by 2 publications

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“…Furthermore, in vitro phosphorylation assays reveal that IC138 is dephosphorylated in response to kinase inhibitors in fla14-3 axonemes indicating that IC97 functions with IC138 in regulation of I1 dynein. Sakakibara et al (2006) have demonstrated that a conformational change occurs in I1 dynein upon phosphorylation. We postulate that this alteration in structure requires the assembly of both IC138 and IC97.…”

Section: Ic97 Is Required For I1-dynein-mediated Control Of Microtubumentioning

confidence: 99%

IC97 Is a Novel Intermediate Chain of I1 Dynein That Interacts with Tubulin and Regulates Interdoublet Sliding

Wirschell

Chun

Yang

et al. 2009

MBoC

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Our goal is to understand the assembly and regulation of flagellar dyneins, particularly the Chlamydomonas inner arm dynein called I1 dynein. Here, we focus on the uncharacterized I1-dynein IC IC97. The IC97 gene encodes a novel IC without notable structural domains. IC97 shares homology with the murine lung adenoma susceptibility 1 (Las1) protein--a candidate tumor suppressor gene implicated in lung tumorigenesis. Multiple, independent biochemical assays determined that IC97 interacts with both alpha- and beta-tubulin subunits within the axoneme. I1-dynein assembly mutants suggest that IC97 interacts with both the IC138 and IC140 subunits within the I1-dynein motor complex and that IC97 is part of a regulatory complex that contains IC138. Microtubule sliding assays, using axonemes containing I1 dynein but devoid of IC97, show reduced microtubule sliding velocities that are not rescued by kinase inhibitors, revealing a critical role for IC97 in I1-dynein function and control of dynein-driven motility.

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Section: Ic97 Is Required For I1-dynein-mediated Control Of Microtubumentioning

confidence: 99%

IC97 Is a Novel Intermediate Chain of I1 Dynein That Interacts with Tubulin and Regulates Interdoublet Sliding

Wirschell

Chun

Yang

et al. 2009

MBoC

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“…I1 dynein forms a two headed structure as revealed by electron microscopy of isolated I1 particles Smith and Sale, 1991;Sakakibara et al, 2006]. Along with the HCs, are three intermediate chains (IC140, IC138, and IC97), and five known light chains (LC) (Tctex1, Tctex2b, LC8, LC7b, and LC7a) Harrison et al, 1998;Perrone et al, 1998;Yang and Sale, 1998;DiBella et al, , 2004aHendrickson et al, 2004;Wirschell et al, 2006] (Fig.…”

Section: Organization Of the Inner Arms: The 96-nm Repeat And Subunitmentioning

confidence: 99%

Keeping an eye on I1: I1 dynein as a model for flagellar dynein assembly and regulation

Wirschell

Hendrickson

Sale

2007

Cell Motil. Cytoskeleton

109

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Among the major challenges in understanding ciliary and flagellar motility is to determine how the dynein motors are assembled and localized and how dyneindriven outer doublet microtubule sliding is controlled. Diverse studies, particularly in Chlamydomonas, have determined that the inner arm dynein I1 is targeted to a unique structural position and is critical for regulating the microtubule sliding required for normal ciliary/flagellar bending. As described in this review, I1 dynein offers additional opportunities to determine the principles of assembly and targeting of dyneins to cellular locations and for studying the mechanisms that regulate dynein activity and control of motility by phosphorylation. Cell Motil.

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2P199 Conformational Changes of Inner-Arm Dynein f from Chlamydomonas Coupled with Phosphorylation of Its Intermediated Chain IC138. III(37. Molecular motor (II),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)

Cited by 2 publications

References 0 publications

IC97 Is a Novel Intermediate Chain of I1 Dynein That Interacts with Tubulin and Regulates Interdoublet Sliding

IC97 Is a Novel Intermediate Chain of I1 Dynein That Interacts with Tubulin and Regulates Interdoublet Sliding

Keeping an eye on I1: I1 dynein as a model for flagellar dynein assembly and regulation

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