Human homologues of the Caenorhabditis elegans cell polarity protein PAR6 as an adaptor that links the small GTPases Rac and Cdc42 to atypical protein kinase C

Yukiko Noda, Ryu Takeya, Shigeo Ohno, Seiji Naito, Takashi Ito, Hideki Sumimoto

研究成果: ジャーナルへの寄稿記事

103 引用 (Scopus)

抄録

Background: Asymmetric cell division in the Caenorhabditis elegans embryos requires products of par (partitioning defective) genes 1-6 and atypical protein kinase C (aPKC), whereas Cdc42 and Rac, members of the Rho family GTPases, play an essential role in cell polarity establishment in yeast and mammalian cells. However, little is known about a link between PAR proteins and the GTPases in cell polarization. Results: Here we have cloned cDNAs for three human homologues of PAR6, designated PAR6α, β and γ, comprising 345, 372 and 376 amino acids, respectively. The PAR6 proteins harbour a PDZ domain and a CRIB-like motif, and directly interact with GTP-bound Rac and Cdc42 via this motif and with the aPKC isoforms PKCι/λ and PKCζ via the N-terminal head-to-head association. These interactions are not mutually exclusive, thereby allowing the PAR6 proteins to form a ternary complex with the GTPases and aPKC, both in vitro and in vivo. When PAR6 and aPKC are expressed with a constitutively active form of Rac in HeLa or COS-7 cells, these proteins co-localize to membrane ruffles, which are known to occur at the leading edge of polarized cells during cell movement. Conclusion: Human PAR6 homologues most likely play an important role in the cell polarization of mammalian cells, by functioning as an adaptor protein that links activated Rac and Cdc42 to aPKC signalling.

元の言語英語
ページ(範囲)107-119
ページ数13
ジャーナルGenes to Cells
6
発行部数2
DOI
出版物ステータス出版済み - 4 17 2001

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Cell Polarity
Monomeric GTP-Binding Proteins
Caenorhabditis elegans
GTP Phosphohydrolases
Proteins
Asymmetric Cell Division
PDZ Domains
rho GTP-Binding Proteins
COS Cells
Guanosine Triphosphate
Cell Movement
Protein Isoforms
Embryonic Structures
Complementary DNA
Yeasts
PKC-3 protein
Amino Acids
Membranes
Genes

All Science Journal Classification (ASJC) codes

  • Genetics
  • Cell Biology

これを引用

Human homologues of the Caenorhabditis elegans cell polarity protein PAR6 as an adaptor that links the small GTPases Rac and Cdc42 to atypical protein kinase C. / Noda, Yukiko; Takeya, Ryu; Ohno, Shigeo; Naito, Seiji; Ito, Takashi; Sumimoto, Hideki.

:: Genes to Cells, 巻 6, 番号 2, 17.04.2001, p. 107-119.

研究成果: ジャーナルへの寄稿記事

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abstract = "Background: Asymmetric cell division in the Caenorhabditis elegans embryos requires products of par (partitioning defective) genes 1-6 and atypical protein kinase C (aPKC), whereas Cdc42 and Rac, members of the Rho family GTPases, play an essential role in cell polarity establishment in yeast and mammalian cells. However, little is known about a link between PAR proteins and the GTPases in cell polarization. Results: Here we have cloned cDNAs for three human homologues of PAR6, designated PAR6α, β and γ, comprising 345, 372 and 376 amino acids, respectively. The PAR6 proteins harbour a PDZ domain and a CRIB-like motif, and directly interact with GTP-bound Rac and Cdc42 via this motif and with the aPKC isoforms PKCι/λ and PKCζ via the N-terminal head-to-head association. These interactions are not mutually exclusive, thereby allowing the PAR6 proteins to form a ternary complex with the GTPases and aPKC, both in vitro and in vivo. When PAR6 and aPKC are expressed with a constitutively active form of Rac in HeLa or COS-7 cells, these proteins co-localize to membrane ruffles, which are known to occur at the leading edge of polarized cells during cell movement. Conclusion: Human PAR6 homologues most likely play an important role in the cell polarization of mammalian cells, by functioning as an adaptor protein that links activated Rac and Cdc42 to aPKC signalling.",
author = "Yukiko Noda and Ryu Takeya and Shigeo Ohno and Seiji Naito and Takashi Ito and Hideki Sumimoto",
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T1 - Human homologues of the Caenorhabditis elegans cell polarity protein PAR6 as an adaptor that links the small GTPases Rac and Cdc42 to atypical protein kinase C

AU - Noda, Yukiko

AU - Takeya, Ryu

AU - Ohno, Shigeo

AU - Naito, Seiji

AU - Ito, Takashi

AU - Sumimoto, Hideki

PY - 2001/4/17

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N2 - Background: Asymmetric cell division in the Caenorhabditis elegans embryos requires products of par (partitioning defective) genes 1-6 and atypical protein kinase C (aPKC), whereas Cdc42 and Rac, members of the Rho family GTPases, play an essential role in cell polarity establishment in yeast and mammalian cells. However, little is known about a link between PAR proteins and the GTPases in cell polarization. Results: Here we have cloned cDNAs for three human homologues of PAR6, designated PAR6α, β and γ, comprising 345, 372 and 376 amino acids, respectively. The PAR6 proteins harbour a PDZ domain and a CRIB-like motif, and directly interact with GTP-bound Rac and Cdc42 via this motif and with the aPKC isoforms PKCι/λ and PKCζ via the N-terminal head-to-head association. These interactions are not mutually exclusive, thereby allowing the PAR6 proteins to form a ternary complex with the GTPases and aPKC, both in vitro and in vivo. When PAR6 and aPKC are expressed with a constitutively active form of Rac in HeLa or COS-7 cells, these proteins co-localize to membrane ruffles, which are known to occur at the leading edge of polarized cells during cell movement. Conclusion: Human PAR6 homologues most likely play an important role in the cell polarization of mammalian cells, by functioning as an adaptor protein that links activated Rac and Cdc42 to aPKC signalling.

AB - Background: Asymmetric cell division in the Caenorhabditis elegans embryos requires products of par (partitioning defective) genes 1-6 and atypical protein kinase C (aPKC), whereas Cdc42 and Rac, members of the Rho family GTPases, play an essential role in cell polarity establishment in yeast and mammalian cells. However, little is known about a link between PAR proteins and the GTPases in cell polarization. Results: Here we have cloned cDNAs for three human homologues of PAR6, designated PAR6α, β and γ, comprising 345, 372 and 376 amino acids, respectively. The PAR6 proteins harbour a PDZ domain and a CRIB-like motif, and directly interact with GTP-bound Rac and Cdc42 via this motif and with the aPKC isoforms PKCι/λ and PKCζ via the N-terminal head-to-head association. These interactions are not mutually exclusive, thereby allowing the PAR6 proteins to form a ternary complex with the GTPases and aPKC, both in vitro and in vivo. When PAR6 and aPKC are expressed with a constitutively active form of Rac in HeLa or COS-7 cells, these proteins co-localize to membrane ruffles, which are known to occur at the leading edge of polarized cells during cell movement. Conclusion: Human PAR6 homologues most likely play an important role in the cell polarization of mammalian cells, by functioning as an adaptor protein that links activated Rac and Cdc42 to aPKC signalling.

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