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Ectodomain shedding, translocation and synthesis of SorLA are stimulated by its ligand head activator

Hampe, Wolfgang, Björn Riedel, I., Lintzel, Julia, Bader, Christian O., Franke, Inga, Schaller, H. Chica·2000·Journal of Cell Science
DOI 10.1242/jcs.113.24.4475
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Abstract

The single transmembrane receptor SorLA is the mammalian orthologue of the head activator-binding protein, HAB, from hydra. The human neuronal precursor cell line NT2 and the neuroendocrine cell line BON produce head activator (HA) and respond to HA by entry into mitosis and cell proliferation. They express SorLA, and bind HA with nanomolar affinity. HA coupled to Sepharose is able to precipitate SorLA specifically proving that SorLA binds HA. Using antisera directed against extra- and intracellular epitopes we find SorLA as membrane receptor and as soluble protein released from cells into the culture medium. Cell lines differ strongly in processing of SorLA, with NT2 cells expressing SorLA mainly as membrane receptor, whereas release predominates in BON cells. Soluble SorLA lacks the intracellular domain and is shed from the transmembrane protein by a metalloprotease. Release from cells and brain slices is stimulated by HA and by phorbol ester, and it is blocked by a metalloprotease inhibitor and by lowering the temperature to 20°C. Blockade of SorLA shedding and treatment of cells with SorLA antisense oligonucleotides lead to a decrease in the rate of cell proliferation. From this we conclude that SorLA is necessary to mediate the mitogenic effect of endogenous HA. HA enhances the translocation of SorLA from internal membranes to the cell surface and its internalization. In addition, HA stimulates SorLA synthesis hinting at an autocatalytic feedback loop in which the ligand activates production, processing, and translocation of its receptor.

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  • Newly synthesized SorLA molecules follow the constitutive secretory pathway from the ER to the cell surface through the Golgi, and undergo post-translational modifications and maturation, resulting in immature and mature species.

    “Newly synthesized SorLA molecules follow the constitutive secretory pathway from the endoplasmic reticulum (ER) to the cell surface, through the Golgi. During their transport through the secretory pathway, SorLA proteins are subjected to several post-translational modifications, including both N- and O-glycosylation, and maturation processes [3–9], resulting in the presence of immature and mature”

    From Impaired SorLA maturation and trafficking as a new mechanism for SORL1 missense variants in Alzheimer disease (2021) · cites this paper as [8]

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Metadata

Authors
Hampe, W., Björn Riedel, I., Lintzel, J., Bader, C. O., Franke, I., & Schaller, H. C.
Venue
Journal of Cell Science
Publisher
The Company of Biologists
Published
2000-12-15
Volume
113
Issue
24
Pages
4475-4485
ISSN
  • 0021-9533
  • 1477-9137
DOI
10.1242/jcs.113.24.4475
Cited by
55
References
1
Language
en
Licence
www.biologists.com/user-licence-1-1/ (vor)

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