Protein 4.1G binds to a unique motif within the Fc gamma RI cytoplasmic tail

J.M. Beekman; J.E. Bakema; C.E. van der Poel; J.A. van der Linden; J.G.J. van de Winkel; J.H.W. Leusen

doi:10.1016/j.molimm.2007.10.024

Protein 4.1G binds to a unique motif within the Fc gamma RI cytoplasmic tail

J.M. Beekman, J.E. Bakema, C.E. van der Poel, J.A. van der Linden, J.G.J. van de Winkel, J.H.W. Leusen

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Abstract

The C-terminal domain of protein 4.1G was identified to interact with the cytosolic tail of the high affinity IgG receptor, Fc gamma RI, in yeast two-hybrid screens. Proteins of the 4.1 family have previously been found to mediate receptor/cytoskeleton interactions. In the study presented here, we show an alternatively spliced 4.1G product to be associated with increased Fc gamma RI binding in yeast two-hybrid assays, and to be selectively enriched in most immune cells at the transcript level. In addition, a detailed analysis of the 4.1G 'docking site' within Fc gamma RI is provided by examining Fc gamma RI-CY-truncated and alanine-substituted mutants. These pointed to an Fc gamma RI membrane-proximal core motif of HxxBxxxBB (H represents hydrophobic residues, B basic residues and x represents any residue), followed by hydrophobic and (potentially) negatively charged residues to be central for interaction with protein 4.1G.

Original language	English
Pages (from-to)	2069-2075
Number of pages	7
Journal	Molecular Immunology
Volume	45
Issue number	7
DOIs	https://doi.org/10.1016/j.molimm.2007.10.024
Publication status	Published - Apr 2008

Keywords

Alternative Splicing
Amino Acid Motifs
Amino Acid Sequence
Animals
Cell Line
Cell Membrane
Cytoplasm
Cytoskeletal Proteins
Humans
Immunoprecipitation
Membrane Proteins
Mice
Molecular Sequence Data
Protein Binding
Protein Interaction Mapping
Protein Structure, Tertiary
RNA, Messenger
Receptors, IgG
Recombinant Proteins
Sequence Homology, Amino Acid
Two-Hybrid System Techniques
Journal Article
Research Support, Non-U.S. Gov't

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@article{9e9013b96464408db09f5d71da15fa50,

title = "Protein 4.1G binds to a unique motif within the Fc gamma RI cytoplasmic tail",

abstract = "The C-terminal domain of protein 4.1G was identified to interact with the cytosolic tail of the high affinity IgG receptor, Fc gamma RI, in yeast two-hybrid screens. Proteins of the 4.1 family have previously been found to mediate receptor/cytoskeleton interactions. In the study presented here, we show an alternatively spliced 4.1G product to be associated with increased Fc gamma RI binding in yeast two-hybrid assays, and to be selectively enriched in most immune cells at the transcript level. In addition, a detailed analysis of the 4.1G 'docking site' within Fc gamma RI is provided by examining Fc gamma RI-CY-truncated and alanine-substituted mutants. These pointed to an Fc gamma RI membrane-proximal core motif of HxxBxxxBB (H represents hydrophobic residues, B basic residues and x represents any residue), followed by hydrophobic and (potentially) negatively charged residues to be central for interaction with protein 4.1G.",

keywords = "Alternative Splicing, Amino Acid Motifs, Amino Acid Sequence, Animals, Cell Line, Cell Membrane, Cytoplasm, Cytoskeletal Proteins, Humans, Immunoprecipitation, Membrane Proteins, Mice, Molecular Sequence Data, Protein Binding, Protein Interaction Mapping, Protein Structure, Tertiary, RNA, Messenger, Receptors, IgG, Recombinant Proteins, Sequence Homology, Amino Acid, Two-Hybrid System Techniques, Journal Article, Research Support, Non-U.S. Gov't",

author = "J.M. Beekman and J.E. Bakema and {van der Poel}, C.E. and {van der Linden}, J.A. and {van de Winkel}, J.G.J. and J.H.W. Leusen",

year = "2008",

month = apr,

doi = "10.1016/j.molimm.2007.10.024",

language = "English",

volume = "45",

pages = "2069--2075",

journal = "Molecular Immunology",

issn = "0161-5890",

publisher = "Elsevier Limited",

number = "7",

}

TY - JOUR

T1 - Protein 4.1G binds to a unique motif within the Fc gamma RI cytoplasmic tail

AU - Beekman, J.M.

AU - Bakema, J.E.

AU - van der Poel, C.E.

AU - van der Linden, J.A.

AU - van de Winkel, J.G.J.

AU - Leusen, J.H.W.

PY - 2008/4

Y1 - 2008/4

N2 - The C-terminal domain of protein 4.1G was identified to interact with the cytosolic tail of the high affinity IgG receptor, Fc gamma RI, in yeast two-hybrid screens. Proteins of the 4.1 family have previously been found to mediate receptor/cytoskeleton interactions. In the study presented here, we show an alternatively spliced 4.1G product to be associated with increased Fc gamma RI binding in yeast two-hybrid assays, and to be selectively enriched in most immune cells at the transcript level. In addition, a detailed analysis of the 4.1G 'docking site' within Fc gamma RI is provided by examining Fc gamma RI-CY-truncated and alanine-substituted mutants. These pointed to an Fc gamma RI membrane-proximal core motif of HxxBxxxBB (H represents hydrophobic residues, B basic residues and x represents any residue), followed by hydrophobic and (potentially) negatively charged residues to be central for interaction with protein 4.1G.

AB - The C-terminal domain of protein 4.1G was identified to interact with the cytosolic tail of the high affinity IgG receptor, Fc gamma RI, in yeast two-hybrid screens. Proteins of the 4.1 family have previously been found to mediate receptor/cytoskeleton interactions. In the study presented here, we show an alternatively spliced 4.1G product to be associated with increased Fc gamma RI binding in yeast two-hybrid assays, and to be selectively enriched in most immune cells at the transcript level. In addition, a detailed analysis of the 4.1G 'docking site' within Fc gamma RI is provided by examining Fc gamma RI-CY-truncated and alanine-substituted mutants. These pointed to an Fc gamma RI membrane-proximal core motif of HxxBxxxBB (H represents hydrophobic residues, B basic residues and x represents any residue), followed by hydrophobic and (potentially) negatively charged residues to be central for interaction with protein 4.1G.

KW - Alternative Splicing

KW - Amino Acid Motifs

KW - Amino Acid Sequence

KW - Animals

KW - Cell Line

KW - Cell Membrane

KW - Cytoplasm

KW - Cytoskeletal Proteins

KW - Humans

KW - Immunoprecipitation

KW - Membrane Proteins

KW - Mice

KW - Molecular Sequence Data

KW - Protein Binding

KW - Protein Interaction Mapping

KW - Protein Structure, Tertiary

KW - RNA, Messenger

KW - Receptors, IgG

KW - Recombinant Proteins

KW - Sequence Homology, Amino Acid

KW - Two-Hybrid System Techniques

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

U2 - 10.1016/j.molimm.2007.10.024

DO - 10.1016/j.molimm.2007.10.024

M3 - Article

C2 - 18023480

SN - 0161-5890

VL - 45

SP - 2069

EP - 2075

JO - Molecular Immunology

JF - Molecular Immunology

IS - 7

ER -

Protein 4.1G binds to a unique motif within the Fc gamma RI cytoplasmic tail

Abstract

Keywords

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