Signaling Through Scaffold, Anchoring, and Adaptor Proteins
Abstract
The process by which extracellular signals are relayed from the plasma membrane to specific intracellular sites is an essential facet of cellular regulation. Many signaling pathways do so by altering the phosphorylation state of tyrosine, serine, or threonine residues of target proteins. Recently, it has become apparent that regulatory mechanisms exist to influence where and when protein kinases and phosphatases are activated in the cell. The role of scaffold, anchoring, and adaptor proteins that contribute to the specificity of signal transduction events by recruiting active enzymes into signaling networks or by placing enzymes close to their substrates is discussed.
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The PPPPY sequence in LRAD3 may also be recognized by molecules containing SH3 domains.
“Interestingly, not only does the PPPPY sequence in LRAD3 conform to the WW domain binding consensus, but this region may also be recognized by molecules containing src homology 3 (SH3) domains (Pawson and Scott, 1997; Pawson, 1995; Cohen et al., 1995).”
From LRAD3, A Novel Low-Density Lipoprotein Receptor Family Member That Modulates Amyloid Precursor Protein Trafficking (2011) · cites this paper as Pawson and Scott, 1997
The cytoplasmic domain of LRAD3 contains two polyproline sequences, SPPSY and PPPPY.
“The cytoplasmic domain of LRAD3 also contains two polyproline sequences, SPPSY, and PPPPY, which represent consensus sequences that are recognized by WW domain containing proteins (Sudol, 1996; Pawson and Scott, 1997).”
From LRAD3, A Novel Low-Density Lipoprotein Receptor Family Member That Modulates Amyloid Precursor Protein Trafficking (2011) · cites this paper as Pawson and Scott, 1997
Many WW domain-containing proteins are involved in regulatory or cell signaling processes.
“The list of proteins that contain WW domains is expanding, and many of these molecules appear to be involved in regulatory or cell signaling processes (Sudol, 1996; Pawson and Scott, 1997).”
From LRAD3, A Novel Low-Density Lipoprotein Receptor Family Member That Modulates Amyloid Precursor Protein Trafficking (2011) · cites this paper as Pawson and Scott, 1997
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“The cytoplasmic domain of LRAD3 also contains two polyproline sequences, SPPSY and PPPPY, which represent consensus sequences that are recognized by WW-domain-containing proteins (Sudol, 1996; Pawson and Scott, 1997).”
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- Authors
- Pawson, T., & Scott, J. D.
- Affiliations
- Mount Sinai Hospital (CA)
- ORCID
- Scott, John D.
- Venue
- Science
- Published
- 1997-12-19
- Volume
- 278
- Issue
- 5346
- Pages
- 2075-2080
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1972172786
- Cited by
- 2,256
- References
- 2
- Citations by year
- 2026: 18 · 2025: 17 · 2024: 29 · 2023: 24 · 2022: 20 · 2021: 36 · 2020: 34 · 2019: 23 · 2018: 30 · 2017: 35 · 2016: 37 · 2015: 47 · 2014: 48 · 2013: 34 · 2012: 63
- FWCI
- 59.48
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (GM-48231)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Keywords
- scaffold proteins, anchoring proteins, adaptor proteins, signal transduction, protein phosphorylation, protein kinases, phosphatase, kinase activation, substrate specificity, plasma membrane signaling
- MeSH terms
- Amino Acid Sequence, Animals, Ligands, Phospholipids, Phosphoprotein Phosphatases, Phosphoproteins, Phosphorylation, Phosphoserine, Phosphothreonine, Protein-Tyrosine Kinases, Proteins, Signal Transduction, Protein Serine-Threonine Kinases, src Homology Domains, Phosphotyrosine
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