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The Conserved Bardet-Biedl Syndrome Proteins Assemble a Coat that Traffics Membrane Proteins to Cilia
The BBSome constitutes a coat complex that sorts membrane proteins to primary cilia and it is proposed that trafficking of BBSome cargoes to cilia entails the coupling ofBBSome coat polymerization to the recognition of sorting signals by the BBSome.
CXCR4 Regulates Interneuron Migration in the Developing Neocortex
These findings suggest that SDF-1, which is highly expressed in the embryonic leptomeninx, selectively regulates migration and layer-specific integration of CXCR4-expressing interneurons during neocortical development.
Regulation of µ-Opioid Receptors: Desensitization, Phosphorylation, Internalization, and Tolerance
- John T. Williams, S. Ingram, +6 authors M. Christie
- Chemistry, MedicinePharmacological Reviews
- 1 January 2013
There are large gaps in understanding the molecular processes responsible for loss of MOR function after chronic exposure to opioids, and further elucidation of the cellular mechanisms that are regulated by opioids will be necessary for the successful development of MOR-based approaches to new pain therapeutics that limit the development of tolerance.
Selective targeting of somatostatin receptor 3 to neuronal cilia
Somatostatin receptor 3 demonstrates a unique example of a G-protein-coupled receptor not localized to "classical" pre- or postsynaptic sites, but selectively targeted to neuronal cilia.
CXCR4 and Gab1 cooperate to control the development of migrating muscle progenitor cells.
- E. Vasyutina, Jürg Stebler, B. Brand-Saberi, S. Schulz, E. Raz, C. Birchmeier
- Biology, MedicineGenes & development
- 15 September 2005
A role of SDF1/CXCR4 signaling in the development of migrating muscle progenitors is revealed and shows that a threshold number of progenitor cells is required to generate muscle of appropriate size.
Cxcr7 Controls Neuronal Migration by Regulating Chemokine Responsiveness
Cxcr7 is necessary to regulate Cxcr4 protein levels, thereby adapting chemokine responsiveness in migrating cells, and this demonstrates that aChemokine receptor modulates the function of another chemokin receptor by controlling the amount of protein that is made available for signaling at the cell surface.
Morphine induces terminal μ‐opioid receptor desensitization by sustained phosphorylation of serine‐375
- S. Schulz, Dana Mayer, M. Pfeiffer, R. Stumm, T. Koch, V. Höllt
- Biology, MedicineThe EMBO journal
- 18 August 2004
It is shown that morphine promotes terminal MOR desensitization by inducing a persistent modification of Ser375, which is a selective phosphorylation of the carboxy‐terminal residue 375.
A Dual Role for the SDF-1/CXCR4 Chemokine Receptor System in Adult Brain: Isoform-Selective Regulation of SDF-1 Expression Modulates CXCR4-Dependent Neuronal Plasticity and Cerebral Leukocyte…
- R. Stumm, Jutta Rummel, +5 authors S. Schulz
- Biology, MedicineThe Journal of Neuroscience
- 15 July 2002
The cellular expression of SDF-1 isoforms and CXCR4 in the brain of mice receiving systemic lipopolysaccharide (LPS) or permanent focal cerebral ischemia is examined to find the isoform-specific regulation of S DF-1 expression modulates neurotransmission and cerebral infiltration via distinct CX CR4-dependent pathways.
Homo- and Heterodimerization of Somatostatin Receptor Subtypes
- M. Pfeiffer, T. Koch, +5 authors S. Schulz
- Biology, MedicineThe Journal of Biological Chemistry
- 27 April 2001
It is shown that the somatostatin receptor (sst) subtypes sst2A and sst3 exist as homodimers at the plasma membrane when expressed in human embryonic kidney 293 cells, and coimmunoprecipitation studies using differentially epitope-tagged receptors are provided, providing direct evidence for heterodimerization of sst 2A andsst3.
Agonist‐selective patterns of µ‐opioid receptor phosphorylation revealed by phosphosite‐specific antibodies
- Christian Doll, J. Konietzko, Florian Pöll, T. Koch, V. Höllt, S. Schulz
- Chemistry, MedicineBritish journal of pharmacology
- 1 September 2011
This work has shown that morphine activates the µ‐opioid receptor without causing its rapid endocytosis, and the detailed molecular events underlying the differential regulation of receptor trafficking by distinct opioid agonists remain incompletely understood.