The scaffold protein c-Jun NH2-terminal kinase-associated leucine zipper protein regulates cell migration through interaction with the G Protein Gα13

Davaakhuu Gantulga, Tuvshintugs Baljinnyam, Yoshio Endo, Takahisa Takino, Hiroshi Sato, Seishi Murakami, Katsuji Yoshioka

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

Scaffold proteins for MAP kinase (MAPK) signalling modules play an important role in the specific and efficient signal transduction of the relevant MAPK cascades. Here, we investigated the function of the scaffolding protein c-Jun NH2-terminal kinase (JNK)-associated leucine zipper protein (JLP) by depleting it in cultured cells using a short hairpin RNA (shRNA) against human JLP. HeLa and DLD-1 cells stably expressing the shRNA showed a defect in cell migration. The re-expression of full-length shRNA-resistant mouse JLP rescued the impaired cell migration of the JLP-depleted HeLa cells; whereas, a C-terminal deletion mutant of mouse JLP, which failed to bind the G protein Gα13, showed little or no effect on the cell migration defect. Furthermore, although a constitutively active Gα13 enhanced the migration of control HeLa cells, the Gα13-induced cell migration was significantly suppressed in the JLP-depleted HeLa cells. Taken together, these results suggest that JLP regulates cell migration through an interaction with Gα13.

Original languageEnglish (US)
Pages (from-to)693-700
Number of pages8
JournalJournal of Biochemistry
Volume144
Issue number6
DOIs
StatePublished - Dec 2008
Externally publishedYes

Fingerprint

G12-G13 GTP-Binding Protein alpha Subunits
Leucine Zippers
JNK Mitogen-Activated Protein Kinases
Scaffolds (biology)
Small Interfering RNA
Cell Movement
Proteins
HeLa Cells
Phosphotransferases
MAP Kinase Signaling System
Signal transduction
Defects
Scaffolds
Cells
Protein Kinases
Cultured Cells
Signal Transduction

Keywords

  • Cell migration
  • MAP kinase
  • p38
  • RNA interference
  • Scaffold protein

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

Cite this

The scaffold protein c-Jun NH2-terminal kinase-associated leucine zipper protein regulates cell migration through interaction with the G Protein Gα13 . / Gantulga, Davaakhuu; Baljinnyam, Tuvshintugs; Endo, Yoshio; Takino, Takahisa; Sato, Hiroshi; Murakami, Seishi; Yoshioka, Katsuji.

In: Journal of Biochemistry, Vol. 144, No. 6, 12.2008, p. 693-700.

Research output: Contribution to journalArticle

Gantulga, Davaakhuu ; Baljinnyam, Tuvshintugs ; Endo, Yoshio ; Takino, Takahisa ; Sato, Hiroshi ; Murakami, Seishi ; Yoshioka, Katsuji. / The scaffold protein c-Jun NH2-terminal kinase-associated leucine zipper protein regulates cell migration through interaction with the G Protein Gα13 . In: Journal of Biochemistry. 2008 ; Vol. 144, No. 6. pp. 693-700.
@article{7264533b2cd34333aed28d6b976e26f8,
title = "The scaffold protein c-Jun NH2-terminal kinase-associated leucine zipper protein regulates cell migration through interaction with the G Protein Gα13",
abstract = "Scaffold proteins for MAP kinase (MAPK) signalling modules play an important role in the specific and efficient signal transduction of the relevant MAPK cascades. Here, we investigated the function of the scaffolding protein c-Jun NH2-terminal kinase (JNK)-associated leucine zipper protein (JLP) by depleting it in cultured cells using a short hairpin RNA (shRNA) against human JLP. HeLa and DLD-1 cells stably expressing the shRNA showed a defect in cell migration. The re-expression of full-length shRNA-resistant mouse JLP rescued the impaired cell migration of the JLP-depleted HeLa cells; whereas, a C-terminal deletion mutant of mouse JLP, which failed to bind the G protein Gα13, showed little or no effect on the cell migration defect. Furthermore, although a constitutively active Gα13 enhanced the migration of control HeLa cells, the Gα13-induced cell migration was significantly suppressed in the JLP-depleted HeLa cells. Taken together, these results suggest that JLP regulates cell migration through an interaction with Gα13.",
keywords = "Cell migration, MAP kinase, p38, RNA interference, Scaffold protein",
author = "Davaakhuu Gantulga and Tuvshintugs Baljinnyam and Yoshio Endo and Takahisa Takino and Hiroshi Sato and Seishi Murakami and Katsuji Yoshioka",
year = "2008",
month = "12",
doi = "10.1093/jb/mvn123",
language = "English (US)",
volume = "144",
pages = "693--700",
journal = "Journal of Biochemistry",
issn = "0021-924X",
publisher = "Oxford University Press",
number = "6",

}

TY - JOUR

T1 - The scaffold protein c-Jun NH2-terminal kinase-associated leucine zipper protein regulates cell migration through interaction with the G Protein Gα13

AU - Gantulga, Davaakhuu

AU - Baljinnyam, Tuvshintugs

AU - Endo, Yoshio

AU - Takino, Takahisa

AU - Sato, Hiroshi

AU - Murakami, Seishi

AU - Yoshioka, Katsuji

PY - 2008/12

Y1 - 2008/12

N2 - Scaffold proteins for MAP kinase (MAPK) signalling modules play an important role in the specific and efficient signal transduction of the relevant MAPK cascades. Here, we investigated the function of the scaffolding protein c-Jun NH2-terminal kinase (JNK)-associated leucine zipper protein (JLP) by depleting it in cultured cells using a short hairpin RNA (shRNA) against human JLP. HeLa and DLD-1 cells stably expressing the shRNA showed a defect in cell migration. The re-expression of full-length shRNA-resistant mouse JLP rescued the impaired cell migration of the JLP-depleted HeLa cells; whereas, a C-terminal deletion mutant of mouse JLP, which failed to bind the G protein Gα13, showed little or no effect on the cell migration defect. Furthermore, although a constitutively active Gα13 enhanced the migration of control HeLa cells, the Gα13-induced cell migration was significantly suppressed in the JLP-depleted HeLa cells. Taken together, these results suggest that JLP regulates cell migration through an interaction with Gα13.

AB - Scaffold proteins for MAP kinase (MAPK) signalling modules play an important role in the specific and efficient signal transduction of the relevant MAPK cascades. Here, we investigated the function of the scaffolding protein c-Jun NH2-terminal kinase (JNK)-associated leucine zipper protein (JLP) by depleting it in cultured cells using a short hairpin RNA (shRNA) against human JLP. HeLa and DLD-1 cells stably expressing the shRNA showed a defect in cell migration. The re-expression of full-length shRNA-resistant mouse JLP rescued the impaired cell migration of the JLP-depleted HeLa cells; whereas, a C-terminal deletion mutant of mouse JLP, which failed to bind the G protein Gα13, showed little or no effect on the cell migration defect. Furthermore, although a constitutively active Gα13 enhanced the migration of control HeLa cells, the Gα13-induced cell migration was significantly suppressed in the JLP-depleted HeLa cells. Taken together, these results suggest that JLP regulates cell migration through an interaction with Gα13.

KW - Cell migration

KW - MAP kinase

KW - p38

KW - RNA interference

KW - Scaffold protein

UR - http://www.scopus.com/inward/record.url?scp=57749174607&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=57749174607&partnerID=8YFLogxK

U2 - 10.1093/jb/mvn123

DO - 10.1093/jb/mvn123

M3 - Article

C2 - 18826971

AN - SCOPUS:57749174607

VL - 144

SP - 693

EP - 700

JO - Journal of Biochemistry

JF - Journal of Biochemistry

SN - 0021-924X

IS - 6

ER -