hnRNP Q regulates Cdc42-mediated neuronal morphogenesis

Hung Hsi Chen, Hsin I. Yu, Wen Cheng Chiang, Yu De Lin, Ben Chang Shia, Woan Yuh Tarn

Research output: Contribution to journalArticle

25 Citations (Scopus)

Abstract

The RNA-binding protein hnRNP Q has been implicated in neuronal mRNA metabolism. Here, we show that knockdown of hnRNP Q increased neurite complexity in cultured rat cortical neurons and induced filopodium formation in mouse neuroblastoma cells. Reexpression of hnRNP Q1 in hnRNP Q-depleted cells abrogated the morphological changes of neurites, indicating a specific role for hnRNP Q1 in neuronal morphogenesis. A search for mRNA targets of hnRNP Q1 identified functionally coherent sets of mRNAs encoding factors involved in cellular signaling or cytoskeletal regulation and determined its preferred binding sequences. We demonstrated that hnRNP Q1 bound to a set of identified mRNAs encoding the components of the actin nucleation-promoting Cdc42/N-WASP/Arp2/3 complex and was in part colocalized with Cdc42 mRNA in granules. Using subcellular fractionation and immunofluorescence, we showed that knockdown of hnRNP Q reduced the level of some of those mRNAs in neurites and redistributed their encoded proteins from neurite tips to soma to different extents. Overexpression of dominant negative mutants of Cdc42 or N-WASP compromised hnRNP Q depletion-induced neurite complexity. Together, our results suggest that hnRNP Q1 may participate in localization of mRNAs encoding Cdc42 signaling factors in neurites, and thereby may regulate actin dynamics and control neuronal morphogenesis.

Original languageEnglish
Pages (from-to)2224-2238
Number of pages15
JournalMolecular and Cellular Biology
Volume32
Issue number12
DOIs
Publication statusPublished - Jun 15 2012
Externally publishedYes

Fingerprint

Heterogeneous-Nuclear Ribonucleoproteins
Morphogenesis
Neurites
Messenger RNA
Actins
Actin-Related Protein 2-3 Complex
Pseudopodia
RNA-Binding Proteins
Carisoprodol
Neuroblastoma
Fluorescent Antibody Technique

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

Cite this

Chen, H. H., Yu, H. I., Chiang, W. C., Lin, Y. D., Shia, B. C., & Tarn, W. Y. (2012). hnRNP Q regulates Cdc42-mediated neuronal morphogenesis. Molecular and Cellular Biology, 32(12), 2224-2238. https://doi.org/10.1128/MCB.06550-11

hnRNP Q regulates Cdc42-mediated neuronal morphogenesis. / Chen, Hung Hsi; Yu, Hsin I.; Chiang, Wen Cheng; Lin, Yu De; Shia, Ben Chang; Tarn, Woan Yuh.

In: Molecular and Cellular Biology, Vol. 32, No. 12, 15.06.2012, p. 2224-2238.

Research output: Contribution to journalArticle

Chen, HH, Yu, HI, Chiang, WC, Lin, YD, Shia, BC & Tarn, WY 2012, 'hnRNP Q regulates Cdc42-mediated neuronal morphogenesis', Molecular and Cellular Biology, vol. 32, no. 12, pp. 2224-2238. https://doi.org/10.1128/MCB.06550-11
Chen, Hung Hsi ; Yu, Hsin I. ; Chiang, Wen Cheng ; Lin, Yu De ; Shia, Ben Chang ; Tarn, Woan Yuh. / hnRNP Q regulates Cdc42-mediated neuronal morphogenesis. In: Molecular and Cellular Biology. 2012 ; Vol. 32, No. 12. pp. 2224-2238.
@article{a16ecae68bb7475fa655a45d2c14aa21,
title = "hnRNP Q regulates Cdc42-mediated neuronal morphogenesis",
abstract = "The RNA-binding protein hnRNP Q has been implicated in neuronal mRNA metabolism. Here, we show that knockdown of hnRNP Q increased neurite complexity in cultured rat cortical neurons and induced filopodium formation in mouse neuroblastoma cells. Reexpression of hnRNP Q1 in hnRNP Q-depleted cells abrogated the morphological changes of neurites, indicating a specific role for hnRNP Q1 in neuronal morphogenesis. A search for mRNA targets of hnRNP Q1 identified functionally coherent sets of mRNAs encoding factors involved in cellular signaling or cytoskeletal regulation and determined its preferred binding sequences. We demonstrated that hnRNP Q1 bound to a set of identified mRNAs encoding the components of the actin nucleation-promoting Cdc42/N-WASP/Arp2/3 complex and was in part colocalized with Cdc42 mRNA in granules. Using subcellular fractionation and immunofluorescence, we showed that knockdown of hnRNP Q reduced the level of some of those mRNAs in neurites and redistributed their encoded proteins from neurite tips to soma to different extents. Overexpression of dominant negative mutants of Cdc42 or N-WASP compromised hnRNP Q depletion-induced neurite complexity. Together, our results suggest that hnRNP Q1 may participate in localization of mRNAs encoding Cdc42 signaling factors in neurites, and thereby may regulate actin dynamics and control neuronal morphogenesis.",
author = "Chen, {Hung Hsi} and Yu, {Hsin I.} and Chiang, {Wen Cheng} and Lin, {Yu De} and Shia, {Ben Chang} and Tarn, {Woan Yuh}",
year = "2012",
month = "6",
day = "15",
doi = "10.1128/MCB.06550-11",
language = "English",
volume = "32",
pages = "2224--2238",
journal = "Molecular and Cellular Biology",
issn = "0270-7306",
publisher = "American Society for Microbiology",
number = "12",

}

TY - JOUR

T1 - hnRNP Q regulates Cdc42-mediated neuronal morphogenesis

AU - Chen, Hung Hsi

AU - Yu, Hsin I.

AU - Chiang, Wen Cheng

AU - Lin, Yu De

AU - Shia, Ben Chang

AU - Tarn, Woan Yuh

PY - 2012/6/15

Y1 - 2012/6/15

N2 - The RNA-binding protein hnRNP Q has been implicated in neuronal mRNA metabolism. Here, we show that knockdown of hnRNP Q increased neurite complexity in cultured rat cortical neurons and induced filopodium formation in mouse neuroblastoma cells. Reexpression of hnRNP Q1 in hnRNP Q-depleted cells abrogated the morphological changes of neurites, indicating a specific role for hnRNP Q1 in neuronal morphogenesis. A search for mRNA targets of hnRNP Q1 identified functionally coherent sets of mRNAs encoding factors involved in cellular signaling or cytoskeletal regulation and determined its preferred binding sequences. We demonstrated that hnRNP Q1 bound to a set of identified mRNAs encoding the components of the actin nucleation-promoting Cdc42/N-WASP/Arp2/3 complex and was in part colocalized with Cdc42 mRNA in granules. Using subcellular fractionation and immunofluorescence, we showed that knockdown of hnRNP Q reduced the level of some of those mRNAs in neurites and redistributed their encoded proteins from neurite tips to soma to different extents. Overexpression of dominant negative mutants of Cdc42 or N-WASP compromised hnRNP Q depletion-induced neurite complexity. Together, our results suggest that hnRNP Q1 may participate in localization of mRNAs encoding Cdc42 signaling factors in neurites, and thereby may regulate actin dynamics and control neuronal morphogenesis.

AB - The RNA-binding protein hnRNP Q has been implicated in neuronal mRNA metabolism. Here, we show that knockdown of hnRNP Q increased neurite complexity in cultured rat cortical neurons and induced filopodium formation in mouse neuroblastoma cells. Reexpression of hnRNP Q1 in hnRNP Q-depleted cells abrogated the morphological changes of neurites, indicating a specific role for hnRNP Q1 in neuronal morphogenesis. A search for mRNA targets of hnRNP Q1 identified functionally coherent sets of mRNAs encoding factors involved in cellular signaling or cytoskeletal regulation and determined its preferred binding sequences. We demonstrated that hnRNP Q1 bound to a set of identified mRNAs encoding the components of the actin nucleation-promoting Cdc42/N-WASP/Arp2/3 complex and was in part colocalized with Cdc42 mRNA in granules. Using subcellular fractionation and immunofluorescence, we showed that knockdown of hnRNP Q reduced the level of some of those mRNAs in neurites and redistributed their encoded proteins from neurite tips to soma to different extents. Overexpression of dominant negative mutants of Cdc42 or N-WASP compromised hnRNP Q depletion-induced neurite complexity. Together, our results suggest that hnRNP Q1 may participate in localization of mRNAs encoding Cdc42 signaling factors in neurites, and thereby may regulate actin dynamics and control neuronal morphogenesis.

UR - http://www.scopus.com/inward/record.url?scp=84864023490&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84864023490&partnerID=8YFLogxK

U2 - 10.1128/MCB.06550-11

DO - 10.1128/MCB.06550-11

M3 - Article

C2 - 22493061

AN - SCOPUS:84864023490

VL - 32

SP - 2224

EP - 2238

JO - Molecular and Cellular Biology

JF - Molecular and Cellular Biology

SN - 0270-7306

IS - 12

ER -