Identification of a novel inhibitory actin-capping protein binding motif in CD2-associated protein

Standard

Identification of a novel inhibitory actin-capping protein binding motif in CD2-associated protein. / Bruck, Serawit; Huber, Tobias B; Ingham, Robert J; Kim, Kyoungtae; Niederstrasser, Hanspeter; Allen, Paul M; Pawson, Tony; Cooper, John A; Shaw, Andrey S.

in: J BIOL CHEM, Jahrgang 281, Nr. 28, 14.07.2006, S. 19196-203.

Publikationen: SCORING: Beitrag in Fachzeitschrift/ZeitungSCORING: ZeitschriftenaufsatzForschungBegutachtung

Harvard

Bruck, S, Huber, TB, Ingham, RJ, Kim, K, Niederstrasser, H, Allen, PM, Pawson, T, Cooper, JA & Shaw, AS 2006, 'Identification of a novel inhibitory actin-capping protein binding motif in CD2-associated protein', J BIOL CHEM, Jg. 281, Nr. 28, S. 19196-203. https://doi.org/10.1074/jbc.M600166200

APA

Bruck, S., Huber, T. B., Ingham, R. J., Kim, K., Niederstrasser, H., Allen, P. M., Pawson, T., Cooper, J. A., & Shaw, A. S. (2006). Identification of a novel inhibitory actin-capping protein binding motif in CD2-associated protein. J BIOL CHEM, 281(28), 19196-203. https://doi.org/10.1074/jbc.M600166200

Vancouver

Bibtex

@article{233e2b678be74d139dcf656b0ffa36c7,
title = "Identification of a novel inhibitory actin-capping protein binding motif in CD2-associated protein",
abstract = "CD2-associated protein (CD2AP) is a scaffold molecule that plays a critical role in the maintenance of the kidney filtration barrier. Little, however, is understood about its mechanism of function. We used mass spectrometry to identify CD2AP-interacting proteins. Many of the proteins that we identified suggest a role for CD2AP in endocytosis and actin regulation. To address the role of CD2AP in regulation of the actin cytoskeleton, we focused on characterizing the interaction of CD2AP with actin-capping protein CP. We identified a novel binding motif LXHXTXXRPK(X)6P present in CD2AP that is also found in its homolog Cin85 and other capping protein-associated proteins such as CARMIL and CKIP-1. CD2AP inhibits the function of capping protein in vitro. Therefore, our results support a role of CD2AP in the regulation of the actin cytoskeleton.",
keywords = "Actins, Adaptor Proteins, Signal Transducing, Amino Acid Motifs, Amino Acid Sequence, Animals, Carrier Proteins, Chickens, Cytoskeletal Proteins, Cytoskeleton, Endocytosis, Humans, Intracellular Signaling Peptides and Proteins, Microfilament Proteins, Molecular Sequence Data, Protein Binding, Proteins, Sequence Homology, Amino Acid, Journal Article, Research Support, N.I.H., Extramural",
author = "Serawit Bruck and Huber, {Tobias B} and Ingham, {Robert J} and Kyoungtae Kim and Hanspeter Niederstrasser and Allen, {Paul M} and Tony Pawson and Cooper, {John A} and Shaw, {Andrey S}",
year = "2006",
month = jul,
day = "14",
doi = "10.1074/jbc.M600166200",
language = "English",
volume = "281",
pages = "19196--203",
journal = "J BIOL CHEM",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "28",

}

RIS

TY - JOUR

T1 - Identification of a novel inhibitory actin-capping protein binding motif in CD2-associated protein

AU - Bruck, Serawit

AU - Huber, Tobias B

AU - Ingham, Robert J

AU - Kim, Kyoungtae

AU - Niederstrasser, Hanspeter

AU - Allen, Paul M

AU - Pawson, Tony

AU - Cooper, John A

AU - Shaw, Andrey S

PY - 2006/7/14

Y1 - 2006/7/14

N2 - CD2-associated protein (CD2AP) is a scaffold molecule that plays a critical role in the maintenance of the kidney filtration barrier. Little, however, is understood about its mechanism of function. We used mass spectrometry to identify CD2AP-interacting proteins. Many of the proteins that we identified suggest a role for CD2AP in endocytosis and actin regulation. To address the role of CD2AP in regulation of the actin cytoskeleton, we focused on characterizing the interaction of CD2AP with actin-capping protein CP. We identified a novel binding motif LXHXTXXRPK(X)6P present in CD2AP that is also found in its homolog Cin85 and other capping protein-associated proteins such as CARMIL and CKIP-1. CD2AP inhibits the function of capping protein in vitro. Therefore, our results support a role of CD2AP in the regulation of the actin cytoskeleton.

AB - CD2-associated protein (CD2AP) is a scaffold molecule that plays a critical role in the maintenance of the kidney filtration barrier. Little, however, is understood about its mechanism of function. We used mass spectrometry to identify CD2AP-interacting proteins. Many of the proteins that we identified suggest a role for CD2AP in endocytosis and actin regulation. To address the role of CD2AP in regulation of the actin cytoskeleton, we focused on characterizing the interaction of CD2AP with actin-capping protein CP. We identified a novel binding motif LXHXTXXRPK(X)6P present in CD2AP that is also found in its homolog Cin85 and other capping protein-associated proteins such as CARMIL and CKIP-1. CD2AP inhibits the function of capping protein in vitro. Therefore, our results support a role of CD2AP in the regulation of the actin cytoskeleton.

KW - Actins

KW - Adaptor Proteins, Signal Transducing

KW - Amino Acid Motifs

KW - Amino Acid Sequence

KW - Animals

KW - Carrier Proteins

KW - Chickens

KW - Cytoskeletal Proteins

KW - Cytoskeleton

KW - Endocytosis

KW - Humans

KW - Intracellular Signaling Peptides and Proteins

KW - Microfilament Proteins

KW - Molecular Sequence Data

KW - Protein Binding

KW - Proteins

KW - Sequence Homology, Amino Acid

KW - Journal Article

KW - Research Support, N.I.H., Extramural

U2 - 10.1074/jbc.M600166200

DO - 10.1074/jbc.M600166200

M3 - SCORING: Journal article

C2 - 16707503

VL - 281

SP - 19196

EP - 19203

JO - J BIOL CHEM

JF - J BIOL CHEM

SN - 0021-9258

IS - 28

ER -