Elipsa is an early determinant of ciliogenesis that links the IFT particle to membrane-associated small GTPase Rab8

Yoshihiro Omori, Chengtian Zhao, Arunesh Saras, Saikat Mukhopadhyay, Woong Kim, Takahisa Furukawa, Piali Sengupta, Alexey Veraksa, Jarema Malicki

Research output: Contribution to journalArticle

142 Citations (Scopus)

Abstract

The formation and function of cilia involves the movement of intraflagellar transport (IFT) particles underneath the ciliary membrane, along axonemal microtubules. Although this process has been studied extensively, its molecular basis remains incompletely understood. For example, it is unknown how the IFT particle interacts with transmembrane proteins. To study the IFT particle further, we examined elipsa, a locus characterized by mutations that cause particularly early ciliogenesis defects in zebrafish. We show here that elipsa encodes a coiled-coil polypeptide that localizes to cilia. Elipsa protein binds to Ift20, a component of IFT particles, and Elipsa homologue in Caenorhabditis elegans, DYF-11, translocates in sensory cilia, similarly to the IFT particle. This indicates that Elipsa is an IFT particle polypeptide. In the context of zebrafish embryogenesis, Elipsa interacts genetically with Rabaptin5, a well-studied regulator of endocytosis, which in turn interacts with Rab8, a small GTPase, known to localize to cilia. We show that Rabaptin5 binds to both Elipsa and Rab8, suggesting that these proteins provide a bridging mechanism between the IFT particle and protein complexes that assemble at the ciliary membrane.

Original languageEnglish (US)
Pages (from-to)437-444
Number of pages8
JournalNature Cell Biology
Volume10
Issue number4
DOIs
StatePublished - 2008

Fingerprint

Monomeric GTP-Binding Proteins
Cilia
Membranes
Zebrafish
Peptides
Proteins
Caenorhabditis elegans
Endocytosis
Microtubules
Embryonic Development
Carrier Proteins
Mutation

ASJC Scopus subject areas

  • Cell Biology

Cite this

Elipsa is an early determinant of ciliogenesis that links the IFT particle to membrane-associated small GTPase Rab8. / Omori, Yoshihiro; Zhao, Chengtian; Saras, Arunesh; Mukhopadhyay, Saikat; Kim, Woong; Furukawa, Takahisa; Sengupta, Piali; Veraksa, Alexey; Malicki, Jarema.

In: Nature Cell Biology, Vol. 10, No. 4, 2008, p. 437-444.

Research output: Contribution to journalArticle

Omori, Y, Zhao, C, Saras, A, Mukhopadhyay, S, Kim, W, Furukawa, T, Sengupta, P, Veraksa, A & Malicki, J 2008, 'Elipsa is an early determinant of ciliogenesis that links the IFT particle to membrane-associated small GTPase Rab8', Nature Cell Biology, vol. 10, no. 4, pp. 437-444. https://doi.org/10.1038/ncb1706
Omori, Yoshihiro ; Zhao, Chengtian ; Saras, Arunesh ; Mukhopadhyay, Saikat ; Kim, Woong ; Furukawa, Takahisa ; Sengupta, Piali ; Veraksa, Alexey ; Malicki, Jarema. / Elipsa is an early determinant of ciliogenesis that links the IFT particle to membrane-associated small GTPase Rab8. In: Nature Cell Biology. 2008 ; Vol. 10, No. 4. pp. 437-444.
@article{5fb3b8256ee54e2c9fc1743b423da8f1,
title = "Elipsa is an early determinant of ciliogenesis that links the IFT particle to membrane-associated small GTPase Rab8",
abstract = "The formation and function of cilia involves the movement of intraflagellar transport (IFT) particles underneath the ciliary membrane, along axonemal microtubules. Although this process has been studied extensively, its molecular basis remains incompletely understood. For example, it is unknown how the IFT particle interacts with transmembrane proteins. To study the IFT particle further, we examined elipsa, a locus characterized by mutations that cause particularly early ciliogenesis defects in zebrafish. We show here that elipsa encodes a coiled-coil polypeptide that localizes to cilia. Elipsa protein binds to Ift20, a component of IFT particles, and Elipsa homologue in Caenorhabditis elegans, DYF-11, translocates in sensory cilia, similarly to the IFT particle. This indicates that Elipsa is an IFT particle polypeptide. In the context of zebrafish embryogenesis, Elipsa interacts genetically with Rabaptin5, a well-studied regulator of endocytosis, which in turn interacts with Rab8, a small GTPase, known to localize to cilia. We show that Rabaptin5 binds to both Elipsa and Rab8, suggesting that these proteins provide a bridging mechanism between the IFT particle and protein complexes that assemble at the ciliary membrane.",
author = "Yoshihiro Omori and Chengtian Zhao and Arunesh Saras and Saikat Mukhopadhyay and Woong Kim and Takahisa Furukawa and Piali Sengupta and Alexey Veraksa and Jarema Malicki",
year = "2008",
doi = "10.1038/ncb1706",
language = "English (US)",
volume = "10",
pages = "437--444",
journal = "Nature Cell Biology",
issn = "1465-7392",
publisher = "Nature Publishing Group",
number = "4",

}

TY - JOUR

T1 - Elipsa is an early determinant of ciliogenesis that links the IFT particle to membrane-associated small GTPase Rab8

AU - Omori, Yoshihiro

AU - Zhao, Chengtian

AU - Saras, Arunesh

AU - Mukhopadhyay, Saikat

AU - Kim, Woong

AU - Furukawa, Takahisa

AU - Sengupta, Piali

AU - Veraksa, Alexey

AU - Malicki, Jarema

PY - 2008

Y1 - 2008

N2 - The formation and function of cilia involves the movement of intraflagellar transport (IFT) particles underneath the ciliary membrane, along axonemal microtubules. Although this process has been studied extensively, its molecular basis remains incompletely understood. For example, it is unknown how the IFT particle interacts with transmembrane proteins. To study the IFT particle further, we examined elipsa, a locus characterized by mutations that cause particularly early ciliogenesis defects in zebrafish. We show here that elipsa encodes a coiled-coil polypeptide that localizes to cilia. Elipsa protein binds to Ift20, a component of IFT particles, and Elipsa homologue in Caenorhabditis elegans, DYF-11, translocates in sensory cilia, similarly to the IFT particle. This indicates that Elipsa is an IFT particle polypeptide. In the context of zebrafish embryogenesis, Elipsa interacts genetically with Rabaptin5, a well-studied regulator of endocytosis, which in turn interacts with Rab8, a small GTPase, known to localize to cilia. We show that Rabaptin5 binds to both Elipsa and Rab8, suggesting that these proteins provide a bridging mechanism between the IFT particle and protein complexes that assemble at the ciliary membrane.

AB - The formation and function of cilia involves the movement of intraflagellar transport (IFT) particles underneath the ciliary membrane, along axonemal microtubules. Although this process has been studied extensively, its molecular basis remains incompletely understood. For example, it is unknown how the IFT particle interacts with transmembrane proteins. To study the IFT particle further, we examined elipsa, a locus characterized by mutations that cause particularly early ciliogenesis defects in zebrafish. We show here that elipsa encodes a coiled-coil polypeptide that localizes to cilia. Elipsa protein binds to Ift20, a component of IFT particles, and Elipsa homologue in Caenorhabditis elegans, DYF-11, translocates in sensory cilia, similarly to the IFT particle. This indicates that Elipsa is an IFT particle polypeptide. In the context of zebrafish embryogenesis, Elipsa interacts genetically with Rabaptin5, a well-studied regulator of endocytosis, which in turn interacts with Rab8, a small GTPase, known to localize to cilia. We show that Rabaptin5 binds to both Elipsa and Rab8, suggesting that these proteins provide a bridging mechanism between the IFT particle and protein complexes that assemble at the ciliary membrane.

UR - http://www.scopus.com/inward/record.url?scp=43149102968&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=43149102968&partnerID=8YFLogxK

U2 - 10.1038/ncb1706

DO - 10.1038/ncb1706

M3 - Article

VL - 10

SP - 437

EP - 444

JO - Nature Cell Biology

JF - Nature Cell Biology

SN - 1465-7392

IS - 4

ER -