Neuronal specific βPix-b stimulates actin-dependent processes via the interaction between its PRD and WH1 domain of N-WASP

Joohyun Park, Yoonju Kim, Zee Yong Park, Dongeun Park, Sunghoe Chang

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3 Citations (Scopus)

Abstract

βPix, a Pak-interacting nucleotide exchange factor (Cool-1/p85SPR), is a Cdc42/Rac1-specific guanine nucleotide exchange factor (GEF) involved in various actin-related processes. Many previous studies have focused on ubiquitously expressed βPix-a, while the role of the neuronal-specific isoform βPix-b is still unknown, especially whether its role is distinct from or similar to βPix-a. Here we show that unlike βPix-a, overexpression of βPix-b stimulates actin-dependent comet formation in BHK21 cells. This effect is attributed to the interaction between its proline-rich domain (PRD) and the WH1 domain of N-WASP. In addition, we show that overexpression of βPix-b stimulates actin-dependent dendritic spine formation in rat hippocampal neurons in culture, a formation that is blocked by co-expression of the WH1 domain of N-WASP or the PRD of βPix-b. Knocking-down endogenous expression of βPix-b by shRNA reduced the number of dendritic spines, which were rescued only by PRD-containing βPix-b mutants. GEF activity of βPix-b is also required for these effects. The results show that neuronal-specific βPix-b stimulates actin-dependent processes in cells via the interaction between its PRD and the WH1 domain of N-WASP. Our results identify N-WASP as the first protein shown to interact with the PRD of βPix-b, raising the possibility that, as an N-WASP WH1-binding protein, βPix-b may regulate N-WASP's activity in cells.

Original languageEnglish
Pages (from-to)1476-1484
Number of pages9
JournalJournal of Cellular Physiology
Volume227
Issue number4
DOIs
StatePublished - 1 Apr 2012

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Proline
Actins
Guanine Nucleotide Exchange Factors
Dendritic Spines
Cell Communication
Small Interfering RNA
Neurons
Rats
Carrier Proteins
Protein Isoforms
Nucleotides
Proteins

Cite this

@article{3c4f30add6844583b57506f6ac130f87,
title = "Neuronal specific βPix-b stimulates actin-dependent processes via the interaction between its PRD and WH1 domain of N-WASP",
abstract = "βPix, a Pak-interacting nucleotide exchange factor (Cool-1/p85SPR), is a Cdc42/Rac1-specific guanine nucleotide exchange factor (GEF) involved in various actin-related processes. Many previous studies have focused on ubiquitously expressed βPix-a, while the role of the neuronal-specific isoform βPix-b is still unknown, especially whether its role is distinct from or similar to βPix-a. Here we show that unlike βPix-a, overexpression of βPix-b stimulates actin-dependent comet formation in BHK21 cells. This effect is attributed to the interaction between its proline-rich domain (PRD) and the WH1 domain of N-WASP. In addition, we show that overexpression of βPix-b stimulates actin-dependent dendritic spine formation in rat hippocampal neurons in culture, a formation that is blocked by co-expression of the WH1 domain of N-WASP or the PRD of βPix-b. Knocking-down endogenous expression of βPix-b by shRNA reduced the number of dendritic spines, which were rescued only by PRD-containing βPix-b mutants. GEF activity of βPix-b is also required for these effects. The results show that neuronal-specific βPix-b stimulates actin-dependent processes in cells via the interaction between its PRD and the WH1 domain of N-WASP. Our results identify N-WASP as the first protein shown to interact with the PRD of βPix-b, raising the possibility that, as an N-WASP WH1-binding protein, βPix-b may regulate N-WASP's activity in cells.",
author = "Joohyun Park and Yoonju Kim and Park, {Zee Yong} and Dongeun Park and Sunghoe Chang",
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language = "English",
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Neuronal specific βPix-b stimulates actin-dependent processes via the interaction between its PRD and WH1 domain of N-WASP. / Park, Joohyun; Kim, Yoonju; Park, Zee Yong; Park, Dongeun; Chang, Sunghoe.

In: Journal of Cellular Physiology, Vol. 227, No. 4, 01.04.2012, p. 1476-1484.

Research output: Contribution to journalArticleResearchpeer-review

TY - JOUR

T1 - Neuronal specific βPix-b stimulates actin-dependent processes via the interaction between its PRD and WH1 domain of N-WASP

AU - Park, Joohyun

AU - Kim, Yoonju

AU - Park, Zee Yong

AU - Park, Dongeun

AU - Chang, Sunghoe

PY - 2012/4/1

Y1 - 2012/4/1

N2 - βPix, a Pak-interacting nucleotide exchange factor (Cool-1/p85SPR), is a Cdc42/Rac1-specific guanine nucleotide exchange factor (GEF) involved in various actin-related processes. Many previous studies have focused on ubiquitously expressed βPix-a, while the role of the neuronal-specific isoform βPix-b is still unknown, especially whether its role is distinct from or similar to βPix-a. Here we show that unlike βPix-a, overexpression of βPix-b stimulates actin-dependent comet formation in BHK21 cells. This effect is attributed to the interaction between its proline-rich domain (PRD) and the WH1 domain of N-WASP. In addition, we show that overexpression of βPix-b stimulates actin-dependent dendritic spine formation in rat hippocampal neurons in culture, a formation that is blocked by co-expression of the WH1 domain of N-WASP or the PRD of βPix-b. Knocking-down endogenous expression of βPix-b by shRNA reduced the number of dendritic spines, which were rescued only by PRD-containing βPix-b mutants. GEF activity of βPix-b is also required for these effects. The results show that neuronal-specific βPix-b stimulates actin-dependent processes in cells via the interaction between its PRD and the WH1 domain of N-WASP. Our results identify N-WASP as the first protein shown to interact with the PRD of βPix-b, raising the possibility that, as an N-WASP WH1-binding protein, βPix-b may regulate N-WASP's activity in cells.

AB - βPix, a Pak-interacting nucleotide exchange factor (Cool-1/p85SPR), is a Cdc42/Rac1-specific guanine nucleotide exchange factor (GEF) involved in various actin-related processes. Many previous studies have focused on ubiquitously expressed βPix-a, while the role of the neuronal-specific isoform βPix-b is still unknown, especially whether its role is distinct from or similar to βPix-a. Here we show that unlike βPix-a, overexpression of βPix-b stimulates actin-dependent comet formation in BHK21 cells. This effect is attributed to the interaction between its proline-rich domain (PRD) and the WH1 domain of N-WASP. In addition, we show that overexpression of βPix-b stimulates actin-dependent dendritic spine formation in rat hippocampal neurons in culture, a formation that is blocked by co-expression of the WH1 domain of N-WASP or the PRD of βPix-b. Knocking-down endogenous expression of βPix-b by shRNA reduced the number of dendritic spines, which were rescued only by PRD-containing βPix-b mutants. GEF activity of βPix-b is also required for these effects. The results show that neuronal-specific βPix-b stimulates actin-dependent processes in cells via the interaction between its PRD and the WH1 domain of N-WASP. Our results identify N-WASP as the first protein shown to interact with the PRD of βPix-b, raising the possibility that, as an N-WASP WH1-binding protein, βPix-b may regulate N-WASP's activity in cells.

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U2 - 10.1002/jcp.22863

DO - 10.1002/jcp.22863

M3 - Article

VL - 227

SP - 1476

EP - 1484

JO - Journal of Cellular Physiology

JF - Journal of Cellular Physiology

SN - 0021-9541

IS - 4

ER -