JSAP1 and JLP are required for ARF6 localization to the midbody in cytokinesis

Tuvshintugs Baljinnyam, Tokiharu Sato, Radnaa Enkhtuya, Katsumi Yamashita, Katsuji Yoshioka

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

The ADP-ribosylation factor 6 (ARF6) GTPase is important in cytokinesis and localizes to the midbody. However, the mechanism and regulation of ARF6's recruitment to the midbody are largely unknown. Here, we investigated the functions of two binding partners of active ARF6, c-Jun NH2-terminal kinase (JNK)/stress-activated protein kinase-associated protein 1 (JSAP1) and JNK-associated leucine zipper protein (JLP), by gene knockout and rescue experiments in mouse embryonic fibroblasts. Depleting both JSAP1 and JLP impaired ARF6's localization to the midbody and delayed cytokinesis. These defects were almost completely rescued by wild-type JSAP1 or JLP, but not by JSAP1 or JLP mutants that were unable to interact with active ARF6 or with the kinesin heavy chain (KHC) of kinesin-1. In transfected cells, a constitutively active form of ARF6 associated with KHC only when co-expressed with wild-type JSAP1 or JLP and not with a JSAP1 or JLP mutant. These findings suggest that JSAP1 and JLP, which might be paralogous to each other, are critical and functionally redundant in cytokinesis and control ARF6 localization to the midbody by forming a tripartite complex of JSAP1/JLP, active ARF6, and kinesin-1.

Original languageEnglish (US)
Pages (from-to)692-703
Number of pages12
JournalGenes to Cells
Volume19
Issue number9
DOIs
StatePublished - 2014
Externally publishedYes

Fingerprint

Leucine Zippers
Cytokinesis
Kinesin
Proteins
JNK Mitogen-Activated Protein Kinases
Mutant Proteins
Gene Knockout Techniques
ADP-ribosylation factor 6
GTP Phosphohydrolases
Heat-Shock Proteins
Protein Kinases
Fibroblasts

ASJC Scopus subject areas

  • Genetics
  • Cell Biology
  • Medicine(all)

Cite this

Baljinnyam, T., Sato, T., Enkhtuya, R., Yamashita, K., & Yoshioka, K. (2014). JSAP1 and JLP are required for ARF6 localization to the midbody in cytokinesis. Genes to Cells, 19(9), 692-703. https://doi.org/10.1111/gtc.12170

JSAP1 and JLP are required for ARF6 localization to the midbody in cytokinesis. / Baljinnyam, Tuvshintugs; Sato, Tokiharu; Enkhtuya, Radnaa; Yamashita, Katsumi; Yoshioka, Katsuji.

In: Genes to Cells, Vol. 19, No. 9, 2014, p. 692-703.

Research output: Contribution to journalArticle

Baljinnyam, T, Sato, T, Enkhtuya, R, Yamashita, K & Yoshioka, K 2014, 'JSAP1 and JLP are required for ARF6 localization to the midbody in cytokinesis', Genes to Cells, vol. 19, no. 9, pp. 692-703. https://doi.org/10.1111/gtc.12170
Baljinnyam, Tuvshintugs ; Sato, Tokiharu ; Enkhtuya, Radnaa ; Yamashita, Katsumi ; Yoshioka, Katsuji. / JSAP1 and JLP are required for ARF6 localization to the midbody in cytokinesis. In: Genes to Cells. 2014 ; Vol. 19, No. 9. pp. 692-703.
@article{8c904eb3312a48e8998e1de97d565faa,
title = "JSAP1 and JLP are required for ARF6 localization to the midbody in cytokinesis",
abstract = "The ADP-ribosylation factor 6 (ARF6) GTPase is important in cytokinesis and localizes to the midbody. However, the mechanism and regulation of ARF6's recruitment to the midbody are largely unknown. Here, we investigated the functions of two binding partners of active ARF6, c-Jun NH2-terminal kinase (JNK)/stress-activated protein kinase-associated protein 1 (JSAP1) and JNK-associated leucine zipper protein (JLP), by gene knockout and rescue experiments in mouse embryonic fibroblasts. Depleting both JSAP1 and JLP impaired ARF6's localization to the midbody and delayed cytokinesis. These defects were almost completely rescued by wild-type JSAP1 or JLP, but not by JSAP1 or JLP mutants that were unable to interact with active ARF6 or with the kinesin heavy chain (KHC) of kinesin-1. In transfected cells, a constitutively active form of ARF6 associated with KHC only when co-expressed with wild-type JSAP1 or JLP and not with a JSAP1 or JLP mutant. These findings suggest that JSAP1 and JLP, which might be paralogous to each other, are critical and functionally redundant in cytokinesis and control ARF6 localization to the midbody by forming a tripartite complex of JSAP1/JLP, active ARF6, and kinesin-1.",
author = "Tuvshintugs Baljinnyam and Tokiharu Sato and Radnaa Enkhtuya and Katsumi Yamashita and Katsuji Yoshioka",
year = "2014",
doi = "10.1111/gtc.12170",
language = "English (US)",
volume = "19",
pages = "692--703",
journal = "Genes to Cells",
issn = "1356-9597",
publisher = "Wiley-Blackwell",
number = "9",

}

TY - JOUR

T1 - JSAP1 and JLP are required for ARF6 localization to the midbody in cytokinesis

AU - Baljinnyam, Tuvshintugs

AU - Sato, Tokiharu

AU - Enkhtuya, Radnaa

AU - Yamashita, Katsumi

AU - Yoshioka, Katsuji

PY - 2014

Y1 - 2014

N2 - The ADP-ribosylation factor 6 (ARF6) GTPase is important in cytokinesis and localizes to the midbody. However, the mechanism and regulation of ARF6's recruitment to the midbody are largely unknown. Here, we investigated the functions of two binding partners of active ARF6, c-Jun NH2-terminal kinase (JNK)/stress-activated protein kinase-associated protein 1 (JSAP1) and JNK-associated leucine zipper protein (JLP), by gene knockout and rescue experiments in mouse embryonic fibroblasts. Depleting both JSAP1 and JLP impaired ARF6's localization to the midbody and delayed cytokinesis. These defects were almost completely rescued by wild-type JSAP1 or JLP, but not by JSAP1 or JLP mutants that were unable to interact with active ARF6 or with the kinesin heavy chain (KHC) of kinesin-1. In transfected cells, a constitutively active form of ARF6 associated with KHC only when co-expressed with wild-type JSAP1 or JLP and not with a JSAP1 or JLP mutant. These findings suggest that JSAP1 and JLP, which might be paralogous to each other, are critical and functionally redundant in cytokinesis and control ARF6 localization to the midbody by forming a tripartite complex of JSAP1/JLP, active ARF6, and kinesin-1.

AB - The ADP-ribosylation factor 6 (ARF6) GTPase is important in cytokinesis and localizes to the midbody. However, the mechanism and regulation of ARF6's recruitment to the midbody are largely unknown. Here, we investigated the functions of two binding partners of active ARF6, c-Jun NH2-terminal kinase (JNK)/stress-activated protein kinase-associated protein 1 (JSAP1) and JNK-associated leucine zipper protein (JLP), by gene knockout and rescue experiments in mouse embryonic fibroblasts. Depleting both JSAP1 and JLP impaired ARF6's localization to the midbody and delayed cytokinesis. These defects were almost completely rescued by wild-type JSAP1 or JLP, but not by JSAP1 or JLP mutants that were unable to interact with active ARF6 or with the kinesin heavy chain (KHC) of kinesin-1. In transfected cells, a constitutively active form of ARF6 associated with KHC only when co-expressed with wild-type JSAP1 or JLP and not with a JSAP1 or JLP mutant. These findings suggest that JSAP1 and JLP, which might be paralogous to each other, are critical and functionally redundant in cytokinesis and control ARF6 localization to the midbody by forming a tripartite complex of JSAP1/JLP, active ARF6, and kinesin-1.

UR - http://www.scopus.com/inward/record.url?scp=84906791469&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84906791469&partnerID=8YFLogxK

U2 - 10.1111/gtc.12170

DO - 10.1111/gtc.12170

M3 - Article

VL - 19

SP - 692

EP - 703

JO - Genes to Cells

JF - Genes to Cells

SN - 1356-9597

IS - 9

ER -