The mammalian formin FHOD1 interacts with the ERK MAP kinase pathway

Matthew B. Boehm, Thomas J. Milius, You Zhou, Jennifer J. Westendorf, Sreenivas Koka

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

Formin homology 2 domain containing protein (FHOD1), a mammalian formin, regulates cytoskeletal architecture, enhances cell migration, and induces gene expression from the serum response element. In this study, we describe co-precipitation of FHOD1 with components of the ERK MAP kinase pathway while co-precipitation of FHOD1 with p38 MAP kinase and JNK was not observed. In addition, FHOD1 co-localized to lamellipodia with Raf-1 and to stress fibers with MEK. FHOD1-induced gene expression from the serum response element was dependent on ERK MAP kinase activation, and the native skeletal actin promoter were activated by FHOD1 through the SRF site. However, FHOD1-induced stress-fiber formation and gene expression from the skeletal actin promoter was independent of ERK activation. These novel data demonstrate that FHOD1-ERK MAP kinase interaction regulates key aspects of FHOD1 biology.

Original languageEnglish (US)
Pages (from-to)1090-1094
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume335
Issue number4
DOIs
StatePublished - Oct 7 2005

Fingerprint

Extracellular Signal-Regulated MAP Kinases
Serum Response Element
Gene expression
Stress Fibers
Coprecipitation
Gene Expression
Actins
Chemical activation
Pseudopodia
Fibers
Mitogen-Activated Protein Kinase Kinases
p38 Mitogen-Activated Protein Kinases
Cell Movement
Proteins

Keywords

  • F-actin
  • FHOD1
  • Formin
  • Gene expression
  • MAP kinase
  • SRE

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

The mammalian formin FHOD1 interacts with the ERK MAP kinase pathway. / Boehm, Matthew B.; Milius, Thomas J.; Zhou, You; Westendorf, Jennifer J.; Koka, Sreenivas.

In: Biochemical and Biophysical Research Communications, Vol. 335, No. 4, 07.10.2005, p. 1090-1094.

Research output: Contribution to journalArticle

Boehm, Matthew B. ; Milius, Thomas J. ; Zhou, You ; Westendorf, Jennifer J. ; Koka, Sreenivas. / The mammalian formin FHOD1 interacts with the ERK MAP kinase pathway. In: Biochemical and Biophysical Research Communications. 2005 ; Vol. 335, No. 4. pp. 1090-1094.
@article{dc40665574fd45368bafe8dcdfda7db0,
title = "The mammalian formin FHOD1 interacts with the ERK MAP kinase pathway",
abstract = "Formin homology 2 domain containing protein (FHOD1), a mammalian formin, regulates cytoskeletal architecture, enhances cell migration, and induces gene expression from the serum response element. In this study, we describe co-precipitation of FHOD1 with components of the ERK MAP kinase pathway while co-precipitation of FHOD1 with p38 MAP kinase and JNK was not observed. In addition, FHOD1 co-localized to lamellipodia with Raf-1 and to stress fibers with MEK. FHOD1-induced gene expression from the serum response element was dependent on ERK MAP kinase activation, and the native skeletal actin promoter were activated by FHOD1 through the SRF site. However, FHOD1-induced stress-fiber formation and gene expression from the skeletal actin promoter was independent of ERK activation. These novel data demonstrate that FHOD1-ERK MAP kinase interaction regulates key aspects of FHOD1 biology.",
keywords = "F-actin, FHOD1, Formin, Gene expression, MAP kinase, SRE",
author = "Boehm, {Matthew B.} and Milius, {Thomas J.} and You Zhou and Westendorf, {Jennifer J.} and Sreenivas Koka",
year = "2005",
month = "10",
day = "7",
doi = "10.1016/j.bbrc.2005.07.191",
language = "English (US)",
volume = "335",
pages = "1090--1094",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "4",

}

TY - JOUR

T1 - The mammalian formin FHOD1 interacts with the ERK MAP kinase pathway

AU - Boehm, Matthew B.

AU - Milius, Thomas J.

AU - Zhou, You

AU - Westendorf, Jennifer J.

AU - Koka, Sreenivas

PY - 2005/10/7

Y1 - 2005/10/7

N2 - Formin homology 2 domain containing protein (FHOD1), a mammalian formin, regulates cytoskeletal architecture, enhances cell migration, and induces gene expression from the serum response element. In this study, we describe co-precipitation of FHOD1 with components of the ERK MAP kinase pathway while co-precipitation of FHOD1 with p38 MAP kinase and JNK was not observed. In addition, FHOD1 co-localized to lamellipodia with Raf-1 and to stress fibers with MEK. FHOD1-induced gene expression from the serum response element was dependent on ERK MAP kinase activation, and the native skeletal actin promoter were activated by FHOD1 through the SRF site. However, FHOD1-induced stress-fiber formation and gene expression from the skeletal actin promoter was independent of ERK activation. These novel data demonstrate that FHOD1-ERK MAP kinase interaction regulates key aspects of FHOD1 biology.

AB - Formin homology 2 domain containing protein (FHOD1), a mammalian formin, regulates cytoskeletal architecture, enhances cell migration, and induces gene expression from the serum response element. In this study, we describe co-precipitation of FHOD1 with components of the ERK MAP kinase pathway while co-precipitation of FHOD1 with p38 MAP kinase and JNK was not observed. In addition, FHOD1 co-localized to lamellipodia with Raf-1 and to stress fibers with MEK. FHOD1-induced gene expression from the serum response element was dependent on ERK MAP kinase activation, and the native skeletal actin promoter were activated by FHOD1 through the SRF site. However, FHOD1-induced stress-fiber formation and gene expression from the skeletal actin promoter was independent of ERK activation. These novel data demonstrate that FHOD1-ERK MAP kinase interaction regulates key aspects of FHOD1 biology.

KW - F-actin

KW - FHOD1

KW - Formin

KW - Gene expression

KW - MAP kinase

KW - SRE

UR - http://www.scopus.com/inward/record.url?scp=24044531287&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=24044531287&partnerID=8YFLogxK

U2 - 10.1016/j.bbrc.2005.07.191

DO - 10.1016/j.bbrc.2005.07.191

M3 - Article

C2 - 16112087

AN - SCOPUS:24044531287

VL - 335

SP - 1090

EP - 1094

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 4

ER -