TY - JOUR
T1 - Aplysia ror forms clusters on the surface of identified neuroendocrine cells
AU - McKay, Sharen E.
AU - Hislop, Jonathan
AU - Scott, Darcy
AU - Bulloch, Andrew G.M.
AU - Kaczmarek, Leonard K.
AU - Carew, Thomas J.
AU - Sossin, Wayne S.
N1 - Funding Information:
We thank Xiaotang Fan for technical assistance. This work was supported by NIMH MH11259 to S.E.M., MRC MT-15121 to W.S.S., NS18492 to L.K.K., MRC MT-7619 to A.G.M.B., and NSF IBN9904608 to T.J.C. W.S.S. is a recipient of a Chercheur-Boursier from Fonds de la Recherche en Sante du Quebec.
PY - 2001
Y1 - 2001
N2 - The ror receptors are a highly conserved family of receptor tyrosine kinases genetically implicated in the establishment of cellular polarity. We have cloned a ror receptor from the marine mollusk Aplysia californica. Aplysia ror (Apror) is expressed in most developing neurons and some adult neuronal populations, including the neuroendocrine bag-cell neurons. The Apror protein is present in peripheral neuronal processes and ganglionic neuropil, implicating the kinase in the regulation of growth and/or synaptic events. In cultured bag-cell neurons, the majority of the protein is stored in intracellular organelles, whereas only a small fraction is expressed on the surface. When expressed on the cell surface, the protein is clustered on neurites, suggesting that Apror is involved in the organization of functional domains within neurons. Apror immunoreactivity partially colocalizes with the P-type calcium channel BC-α1A at bag-cell neuron varicosities, suggesting a role for Apror in organizing neuropeptide release sites.
AB - The ror receptors are a highly conserved family of receptor tyrosine kinases genetically implicated in the establishment of cellular polarity. We have cloned a ror receptor from the marine mollusk Aplysia californica. Aplysia ror (Apror) is expressed in most developing neurons and some adult neuronal populations, including the neuroendocrine bag-cell neurons. The Apror protein is present in peripheral neuronal processes and ganglionic neuropil, implicating the kinase in the regulation of growth and/or synaptic events. In cultured bag-cell neurons, the majority of the protein is stored in intracellular organelles, whereas only a small fraction is expressed on the surface. When expressed on the cell surface, the protein is clustered on neurites, suggesting that Apror is involved in the organization of functional domains within neurons. Apror immunoreactivity partially colocalizes with the P-type calcium channel BC-α1A at bag-cell neuron varicosities, suggesting a role for Apror in organizing neuropeptide release sites.
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U2 - 10.1006/mcne.2001.0977
DO - 10.1006/mcne.2001.0977
M3 - Article
C2 - 11358481
AN - SCOPUS:0034992269
SN - 1044-7431
VL - 17
SP - 821
EP - 841
JO - Molecular and Cellular Neuroscience
JF - Molecular and Cellular Neuroscience
IS - 5
ER -