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Switching Signals On or Off by Receptor Dimerization
Abstract
Many extracellular signals transduce their cellular responses by regulating the tyrosine phosphorylation of target proteins. Protein tyrosine kinases (PTKs) can be divided into two classes of enzymes: receptor PTKs that span a membrane, and cytoplasmic PTKs. Conversely, the dephosphorylation reaction of tyrosine phosphorylated proteins is carried out by protein tyrosine phosphatases (PTPs). PTPs can also be divided into two classes of enzymes: transmembrane receptor-like PTPs, and cytoplasmic PTPs. Considerable progress has been made in understanding the regulation and activation of PTKs. In contrast, very little is known about the regulation and activity of PTPs, although a few clues are emerging from recent structural and functional studies. Some of the paradigms learned from studying the PTKs have guided us well in our efforts toward understanding PTP function. However, some surprising differences are also suggested.
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Physiological ligands may activate LRP1 and related receptors by binding two or more receptor molecules, resulting in dimerization of the intracellular domain, leading to phosphorylation of tyrosine residues in these domains, which in turn recruit other signaling or scaffolding proteins.
“Physiological ligands may activate LRP1 and related receptors by binding two or more receptor molecules, resulting in dimerization of the intracellular domain, leading to phosphorylation of tyrosine residues in these domains, which in turn recruit other signaling or scaffolding proteins (51).”
From LRPAP1 is released from activated microglia and inhibits microglial phagocytosis and amyloid beta aggregation (2023) · cites this paper as [51]
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Metadata
- Authors
- Weiss, A., & Schlessinger, J.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1998-08
- Volume
- 94
- Issue
- 3
- Pages
- 277-280
- ISSN
- 0092-8674
- Cited by
- 355
- References
- 0
- Language
- en
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