Sorting by the Cytoplasmic Domain of the Amyloid Precursor Protein Binding Receptor SorLA

Nielsen, Morten S.; Gustafsen, Camilla; Madsen, Peder; Nyengaard, Jens R.; Hermey, Guido; Bakke, Oddmund; Mari, Muriel; Schu, Peter; Pohlmann, Regina; Dennes, André; Petersen, Claus M.

doi:10.1128/mcb.00815-07

Cited by 184

The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.

Sorting by the Cytoplasmic Domain of the Amyloid Precursor Protein Binding Receptor SorLA

Nielsen, Morten S., Gustafsen, Camilla, Madsen, Peder, Nyengaard, Jens R., Hermey, Guido, Bakke, Oddmund, Mari, Muriel, Schu, Peter, Pohlmann, Regina, Dennes, André, Petersen, Claus M.·2007·Molecular and Cellular Biology

DOI 10.1128/mcb.00815-07

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Abstract

SorLA/LR11 (250 kDa) is the largest and most composite member of the Vps10p-domain receptors, a family of type 1 proteins preferentially expressed in neuronal tissue. SorLA binds several ligands, including neurotensin, platelet-derived growth factor-bb, and lipoprotein lipase, and via complex-formation with the amyloid precursor protein it downregulates generation of Alzheimer's disease-associated Abeta-peptide. The receptor is mainly located in vesicles, suggesting a function in protein sorting and transport. Here we examined SorLA's trafficking using full-length and chimeric receptors and find that its cytoplasmic tail mediates efficient Golgi body-endosome transport, as well as AP-2 complex-dependent endocytosis. Functional sorting sites were mapped to an acidic cluster-dileucine-like motif and to a GGA binding site in the C terminus. Experiments in permanently or transiently AP-1 mu1-chain-deficient cells established that the AP-1 adaptor complex is essential to SorLA's transport between Golgi membranes and endosomes. Our results further implicate the GGA proteins in SorLA trafficking and provide evidence that SNX1 and Vps35, as parts of the retromer complex or possibly in a separate context, are engaged in retraction of the receptor from endosomes.

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In wild-type hiPSCs, SorLA immunostaining reveals a polarized localization in large perinuclear vesicles and in smaller vesicles dispersed throughout the cytoplasm.
“In accordance with previous reports [11, 41, 42], SorLA immunostaining in wild-type hiPSCs revealed a polarized localization, both in large perinuclear vesicles, and in smaller vesicles dispersed throughout the cytoplasm (Fig. 6).”
From Impaired SorLA maturation and trafficking as a new mechanism for SORL1 missense variants in Alzheimer disease (2021) · cites this paper as [11]
Retromer and its receptors, SORLA and CIMPR, function to traffic mature lysosomal hydrolases from the TGN via endosomes to lysosomes.
“In particular, retromer and its receptors, SORLA and the cation‐independent mannose‐6 phosphate receptor (CIMPR), function to traffic mature lysosomal hydrolases from the TGN via endosomes to lysosomes (Cui et al. 2019; Hasanagic et al. 2015; Nielsen et al. 2007).”
From The Alzheimer's Disease Gene SORL1 Regulates Lysosome Function in Human Microglia (2025) · cites this paper as Nielsen et al. 2007

Lipoprotein receptors in the nervous system
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The sortilin cytoplasmic tail conveys Golgi–endosome transport and binds the VHS domain of the GGA2 sorting protein
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Self-citation
Molecular Dissection of the Interaction between Amyloid Precursor Protein and Its Neuronal Trafficking Receptor SorLA/LR11
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Self-citation
The mosaic receptor sorLA/LR11 binds components of the plasminogen-activating system and platelet-derived growth factor-BB similarly to LRP1 (low-density lipoprotein receptor-related protein), but mediates slow internalization of bound ligand
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Sorted by citations

Linking Aβ and Tau in Late-Onset Alzheimer's Disease: A Dual Pathway Hypothesis
Small, S. A., & Duff, K. (2008) · Neuron · doi:10.1016/j.neuron.2008.11.007 · Cited by 546
Endosomal retrieval of cargo: Retromer is not alone
McNally, K. E., & Cullen, P. J. (2018) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.06.005 · Cited by 169
Lysosome biogenesis in health and disease
Bajaj, L., Lotfi, P., Pal, R., Ronza, A. D., Sharma, J., & Sardiello, M. (2019) · Journal of Neurochemistry · doi:10.1111/jnc.14564 · Cited by 153
The Role of SORL1 in Alzheimer’s Disease
Yin, R.-H., Yu, J.-T., & Tan, L. (2015) · Molecular Neurobiology · doi:10.1007/s12035-014-8742-5 · Cited by 126
Impaired SorLA maturation and trafficking as a new mechanism for SORL1 missense variants in Alzheimer disease
Rovelet-Lecrux, A., Feuillette, S., Miguel, L., Schramm, C., Pernet, S., Quenez, O., Ségalas-Milazzo, I., Guilhaudis, L., Rousseau, S., Riou, G., et al. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01294-4 · Cited by 38
The Alzheimer's Disease Gene SORL1 Regulates Lysosome Function in Human Microglia
Mishra, S., Morshed, N., Sidhu, S. B., Kinoshita, C., Stevens, B., Jayadev, S., & Young, J. E. (2025) · Glia · doi:10.1002/glia.70009 · Cited by 31

Authors: Nielsen, M. S., Gustafsen, C., Madsen, P., Nyengaard, J. R., Hermey, G., Bakke, O., Mari, M., Schu, P., Pohlmann, R., Dennes, A., & Petersen, C. M.
Venue: Molecular and Cellular Biology
Publisher: Informa UK Limited
Published: 2007-10-01
Volume: 27
Issue: 19
Pages: 6842-6851
ISSN: 1098-5549
DOI: 10.1128/mcb.00815-07
Cited by: 184
References: 5
Language: en
Licence: journals.asm.org/non-commercial-tdm-license (tdm)

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Sorting by the Cytoplasmic Domain of the Amyloid Precursor Protein Binding Receptor SorLA

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