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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 interaction partners of SLAP-1 (pink) and SLAP-2 (green). Several proteins have been reported to interact with SLAP-1 molecule: c-Cbl, CD3 ζ chain, ECK, EpoR, Igα, LAT, Lck, PDGFR, SLP-76, Syk, v-abl, Vav (protooncogene vav), ZAP70, c-kit, Flt3, and FLI. SLAP-2 interacts with c-Cbl, CD3 ζ chain, CSFR, and ZAP70.
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fig2: The interaction partners of SLAP-1 (pink) and SLAP-2 (green). Several proteins have been reported to interact with SLAP-1 molecule: c-Cbl, CD3 ζ chain, ECK, EpoR, Igα, LAT, Lck, PDGFR, SLP-76, Syk, v-abl, Vav (protooncogene vav), ZAP70, c-kit, Flt3, and FLI. SLAP-2 interacts with c-Cbl, CD3 ζ chain, CSFR, and ZAP70.

Mentions: Human SLAP-1 and SLAP-2 molecules show sequence homology similarly to mouse SLAP proteins. SH domains are the most similar parts of the two SLAP molecules, in which the sequence homology is 59%, while the N-terminals are the most different parts; they have only 19% identity. SLAP-2 has a shorter alternative splice variant, called SLAP-2v. This isoform contains only 210 amino acids due to the deletion of 50 bp from exon 6, which results an alternative reading frame. The splicing variant molecule does not have any c-Cbl interacting site. The biological relevance of SLAP-2v is yet unknown [5, 6]. Although expression of SLAP-1 and SLAP-2 mRNAs has been most extensively studied in lymphocytes, they are also expressed by numerous human and murine tissues and cell lines [1, 2, 7–12] (Table 1). Several proteins have been reported to interact with SLAP-1 and SLAP-2 [5, 8, 9, 13–15] (Figure 2). SLAPs are involved in a broad range of cellular processes, for example, lymphocyte development, neuronal excitotoxicity and platelet activation. SLAP molecules may participate in several pathological conditions of the immune system as well. In the present review, we will discuss the role of both SLAP proteins in different cell types and overview our current understanding regarding their relevance in pathological conditions.


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 interaction partners of SLAP-1 (pink) and SLAP-2 (green). Several proteins have been reported to interact with SLAP-1 molecule: c-Cbl, CD3 ζ chain, ECK, EpoR, Igα, LAT, Lck, PDGFR, SLP-76, Syk, v-abl, Vav (protooncogene vav), ZAP70, c-kit, Flt3, and FLI. SLAP-2 interacts with c-Cbl, CD3 ζ chain, CSFR, and ZAP70.
© Copyright Policy - open-access
Related In: Results  -  Collection

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

fig2: The interaction partners of SLAP-1 (pink) and SLAP-2 (green). Several proteins have been reported to interact with SLAP-1 molecule: c-Cbl, CD3 ζ chain, ECK, EpoR, Igα, LAT, Lck, PDGFR, SLP-76, Syk, v-abl, Vav (protooncogene vav), ZAP70, c-kit, Flt3, and FLI. SLAP-2 interacts with c-Cbl, CD3 ζ chain, CSFR, and ZAP70.
Mentions: Human SLAP-1 and SLAP-2 molecules show sequence homology similarly to mouse SLAP proteins. SH domains are the most similar parts of the two SLAP molecules, in which the sequence homology is 59%, while the N-terminals are the most different parts; they have only 19% identity. SLAP-2 has a shorter alternative splice variant, called SLAP-2v. This isoform contains only 210 amino acids due to the deletion of 50 bp from exon 6, which results an alternative reading frame. The splicing variant molecule does not have any c-Cbl interacting site. The biological relevance of SLAP-2v is yet unknown [5, 6]. Although expression of SLAP-1 and SLAP-2 mRNAs has been most extensively studied in lymphocytes, they are also expressed by numerous human and murine tissues and cell lines [1, 2, 7–12] (Table 1). Several proteins have been reported to interact with SLAP-1 and SLAP-2 [5, 8, 9, 13–15] (Figure 2). SLAPs are involved in a broad range of cellular processes, for example, lymphocyte development, neuronal excitotoxicity and platelet activation. SLAP molecules may participate in several pathological conditions of the immune system as well. In the present review, we will discuss the role of both SLAP proteins in different cell types and overview our current understanding regarding their relevance in pathological conditions.

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