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The Emerging and Diverse Roles of Src-Like Adaptor Proteins in Health and Disease.

Marton N, Baricza E, Érsek B, Buzás EI, Nagy G - Mediators Inflamm. (2015)

Bottom Line: Although Src-like adaptor proteins (SLAP-1 and SLAP-2) were mainly studied in lymphocytes, where they act as negative regulators and provide fine control of receptor signaling, recently, several other functions of these proteins were discovered.Both adaptor proteins are expressed in a wide variety of tissues, where they have mostly inhibitory effects on multiple intracellular signaling pathways.In this review, we summarize the diverse effects of SLAP proteins.

View Article: PubMed Central - PubMed

Affiliation: Department of Genetics, Cell- and Immunobiology, Semmelweis University, 4 Nagyvárad Square, Budapest 1089, Hungary.

ABSTRACT
Although Src-like adaptor proteins (SLAP-1 and SLAP-2) were mainly studied in lymphocytes, where they act as negative regulators and provide fine control of receptor signaling, recently, several other functions of these proteins were discovered. In addition to the well-characterized immunoregulatory functions, SLAP proteins appear to have an essential role in the pathogenesis of type I hypersensitivity, osteoporosis, and numerous malignant diseases. Both adaptor proteins are expressed in a wide variety of tissues, where they have mostly inhibitory effects on multiple intracellular signaling pathways. In this review, we summarize the diverse effects of SLAP proteins.

No MeSH data available.


Related in: MedlinePlus

The schematic structure of SLAP molecules. SLAP-1 and SLAP-2 contain unique carboxy-terminal sequences, common SH2-SH3 domains and amino-terminals which exist in myristoylated and nonmyristoylated isoforms. SH2 domains help molecules to bind to phosphorylated tyrosine containing epitopes. The SH3 domains connect the proline and hydrophobic amino acid containing molecules.
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fig1: The schematic structure of SLAP molecules. SLAP-1 and SLAP-2 contain unique carboxy-terminal sequences, common SH2-SH3 domains and amino-terminals which exist in myristoylated and nonmyristoylated isoforms. SH2 domains help molecules to bind to phosphorylated tyrosine containing epitopes. The SH3 domains connect the proline and hydrophobic amino acid containing molecules.

Mentions: Signal transducing adaptor proteins are a group of intracellular and transmembrane molecules which are crucial supplementary factors of signaling pathways. They mediate interactions between different molecules and contribute to the formation of signaling complexes. Adaptor proteins lack enzymatic activity and interaction domains enable them to connect with other molecules (e.g., proteins, lipids). Src-like adaptor protein 1 (SLAP-1) was cloned in a yeast two-hybrid screen with the cytoplasmic domain of the receptor tyrosine kinase ephrin type-A receptor 2 as decoy [1, 2]. SLAP proteins are not identical in size; SLAP-1 (or often quoted as SLAP) contains 276 amino acids while SLAP-2 consists of 261 amino acids (Figure 1). SLAP-1 and SLAP-2 contain common SH2-SH3 domains. SH2 domains allow proteins to dock to phosphorylated tyrosine containing epitopes. SH3 domains bind to hydrophobic amino acid and proline rich molecules. SH domains of SLAP-2 form continuous β-sheet that stretches the modular domains [3].


The Emerging and Diverse Roles of Src-Like Adaptor Proteins in Health and Disease.

Marton N, Baricza E, Érsek B, Buzás EI, Nagy G - Mediators Inflamm. (2015)

The schematic structure of SLAP molecules. SLAP-1 and SLAP-2 contain unique carboxy-terminal sequences, common SH2-SH3 domains and amino-terminals which exist in myristoylated and nonmyristoylated isoforms. SH2 domains help molecules to bind to phosphorylated tyrosine containing epitopes. The SH3 domains connect the proline and hydrophobic amino acid containing molecules.
© Copyright Policy - open-access
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC4539169&req=5

fig1: The schematic structure of SLAP molecules. SLAP-1 and SLAP-2 contain unique carboxy-terminal sequences, common SH2-SH3 domains and amino-terminals which exist in myristoylated and nonmyristoylated isoforms. SH2 domains help molecules to bind to phosphorylated tyrosine containing epitopes. The SH3 domains connect the proline and hydrophobic amino acid containing molecules.
Mentions: Signal transducing adaptor proteins are a group of intracellular and transmembrane molecules which are crucial supplementary factors of signaling pathways. They mediate interactions between different molecules and contribute to the formation of signaling complexes. Adaptor proteins lack enzymatic activity and interaction domains enable them to connect with other molecules (e.g., proteins, lipids). Src-like adaptor protein 1 (SLAP-1) was cloned in a yeast two-hybrid screen with the cytoplasmic domain of the receptor tyrosine kinase ephrin type-A receptor 2 as decoy [1, 2]. SLAP proteins are not identical in size; SLAP-1 (or often quoted as SLAP) contains 276 amino acids while SLAP-2 consists of 261 amino acids (Figure 1). SLAP-1 and SLAP-2 contain common SH2-SH3 domains. SH2 domains allow proteins to dock to phosphorylated tyrosine containing epitopes. SH3 domains bind to hydrophobic amino acid and proline rich molecules. SH domains of SLAP-2 form continuous β-sheet that stretches the modular domains [3].

Bottom Line: Although Src-like adaptor proteins (SLAP-1 and SLAP-2) were mainly studied in lymphocytes, where they act as negative regulators and provide fine control of receptor signaling, recently, several other functions of these proteins were discovered.Both adaptor proteins are expressed in a wide variety of tissues, where they have mostly inhibitory effects on multiple intracellular signaling pathways.In this review, we summarize the diverse effects of SLAP proteins.

View Article: PubMed Central - PubMed

Affiliation: Department of Genetics, Cell- and Immunobiology, Semmelweis University, 4 Nagyvárad Square, Budapest 1089, Hungary.

ABSTRACT
Although Src-like adaptor proteins (SLAP-1 and SLAP-2) were mainly studied in lymphocytes, where they act as negative regulators and provide fine control of receptor signaling, recently, several other functions of these proteins were discovered. In addition to the well-characterized immunoregulatory functions, SLAP proteins appear to have an essential role in the pathogenesis of type I hypersensitivity, osteoporosis, and numerous malignant diseases. Both adaptor proteins are expressed in a wide variety of tissues, where they have mostly inhibitory effects on multiple intracellular signaling pathways. In this review, we summarize the diverse effects of SLAP proteins.

No MeSH data available.


Related in: MedlinePlus