The myosin I SH3 domain and TEDS rule phosphorylation site are required for in vivo function

Kristine D. Novak, Margaret A. Titus

Research output: Contribution to journalArticle

53 Citations (Scopus)

Abstract

The class I myosins play important roles in controlling many different types of actin-based cell movements. Dictyostelium cells either lacking or overexpressing amoeboid myosin Is have significant defects in cortical activities such as pseudopod extension, cell migration, and macropinocytosis. The existence of Dictyostelium null mutants with strong phenotypic defects permits complementation analysis as a means of exploring important functional features of the myosin I heavy chain. Mutant Dictyostelium cells lacking two myosin Is exhibit profound defects in growth, endocytosis, and rearrangement of F-actin. Expression of the full-length myoB heavy chain in these cells fully rescues the double mutant defects. However, mutant forms of the myoB heavy chain in which a serine at the consensus phosphorylation site has been altered to an alanine or in which the C-terminal SH3 domain has been removed fail to complement the null phenotype. The wild-type and mutant forms of the myoB heavy chain appeared to be properly localized when they were expressed in the myosin I null mutants. These results suggest that the amoeboid myosin I consensus phosphorylation site and SH3 domains do not play a role in the localization of myosin I, but are absolutely required for in vivo function.

Original languageEnglish (US)
Pages (from-to)75-88
Number of pages14
JournalMolecular Biology of the Cell
Volume9
Issue number1
DOIs
StatePublished - Jan 1 1998

Fingerprint

Myosin Type I
src Homology Domains
Phosphorylation
Dictyostelium
Myosins
Cell Movement
Actins
Pseudopodia
Myosin Heavy Chains
Endocytosis
Alanine
Serine
Phenotype
Growth

Cite this

The myosin I SH3 domain and TEDS rule phosphorylation site are required for in vivo function. / Novak, Kristine D.; Titus, Margaret A.

In: Molecular Biology of the Cell, Vol. 9, No. 1, 01.01.1998, p. 75-88.

Research output: Contribution to journalArticle

@article{551fd81bbeda4ad1a10d35cea210fda6,
title = "The myosin I SH3 domain and TEDS rule phosphorylation site are required for in vivo function",
abstract = "The class I myosins play important roles in controlling many different types of actin-based cell movements. Dictyostelium cells either lacking or overexpressing amoeboid myosin Is have significant defects in cortical activities such as pseudopod extension, cell migration, and macropinocytosis. The existence of Dictyostelium null mutants with strong phenotypic defects permits complementation analysis as a means of exploring important functional features of the myosin I heavy chain. Mutant Dictyostelium cells lacking two myosin Is exhibit profound defects in growth, endocytosis, and rearrangement of F-actin. Expression of the full-length myoB heavy chain in these cells fully rescues the double mutant defects. However, mutant forms of the myoB heavy chain in which a serine at the consensus phosphorylation site has been altered to an alanine or in which the C-terminal SH3 domain has been removed fail to complement the null phenotype. The wild-type and mutant forms of the myoB heavy chain appeared to be properly localized when they were expressed in the myosin I null mutants. These results suggest that the amoeboid myosin I consensus phosphorylation site and SH3 domains do not play a role in the localization of myosin I, but are absolutely required for in vivo function.",
author = "Novak, {Kristine D.} and Titus, {Margaret A.}",
year = "1998",
month = "1",
day = "1",
doi = "10.1091/mbc.9.1.75",
language = "English (US)",
volume = "9",
pages = "75--88",
journal = "Molecular Biology of the Cell",
issn = "1059-1524",
publisher = "American Society for Cell Biology",
number = "1",

}

TY - JOUR

T1 - The myosin I SH3 domain and TEDS rule phosphorylation site are required for in vivo function

AU - Novak, Kristine D.

AU - Titus, Margaret A.

PY - 1998/1/1

Y1 - 1998/1/1

N2 - The class I myosins play important roles in controlling many different types of actin-based cell movements. Dictyostelium cells either lacking or overexpressing amoeboid myosin Is have significant defects in cortical activities such as pseudopod extension, cell migration, and macropinocytosis. The existence of Dictyostelium null mutants with strong phenotypic defects permits complementation analysis as a means of exploring important functional features of the myosin I heavy chain. Mutant Dictyostelium cells lacking two myosin Is exhibit profound defects in growth, endocytosis, and rearrangement of F-actin. Expression of the full-length myoB heavy chain in these cells fully rescues the double mutant defects. However, mutant forms of the myoB heavy chain in which a serine at the consensus phosphorylation site has been altered to an alanine or in which the C-terminal SH3 domain has been removed fail to complement the null phenotype. The wild-type and mutant forms of the myoB heavy chain appeared to be properly localized when they were expressed in the myosin I null mutants. These results suggest that the amoeboid myosin I consensus phosphorylation site and SH3 domains do not play a role in the localization of myosin I, but are absolutely required for in vivo function.

AB - The class I myosins play important roles in controlling many different types of actin-based cell movements. Dictyostelium cells either lacking or overexpressing amoeboid myosin Is have significant defects in cortical activities such as pseudopod extension, cell migration, and macropinocytosis. The existence of Dictyostelium null mutants with strong phenotypic defects permits complementation analysis as a means of exploring important functional features of the myosin I heavy chain. Mutant Dictyostelium cells lacking two myosin Is exhibit profound defects in growth, endocytosis, and rearrangement of F-actin. Expression of the full-length myoB heavy chain in these cells fully rescues the double mutant defects. However, mutant forms of the myoB heavy chain in which a serine at the consensus phosphorylation site has been altered to an alanine or in which the C-terminal SH3 domain has been removed fail to complement the null phenotype. The wild-type and mutant forms of the myoB heavy chain appeared to be properly localized when they were expressed in the myosin I null mutants. These results suggest that the amoeboid myosin I consensus phosphorylation site and SH3 domains do not play a role in the localization of myosin I, but are absolutely required for in vivo function.

UR - http://www.scopus.com/inward/record.url?scp=0031933790&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0031933790&partnerID=8YFLogxK

U2 - 10.1091/mbc.9.1.75

DO - 10.1091/mbc.9.1.75

M3 - Article

VL - 9

SP - 75

EP - 88

JO - Molecular Biology of the Cell

JF - Molecular Biology of the Cell

SN - 1059-1524

IS - 1

ER -