Structure of WNT inhibitor adenomatosis polyposis coli down-regulated 1 (APCDD1), a cell-surface lipid-binding protein

Hsieh, Fu-Lien; Chang, Tao-Hsin; Gabelli, Sandra B.; Nathans, Jeremy

doi:10.1073/pnas.2217096120

Title: Structure of WNT inhibitor adenomatosis polyposis coli down-regulated 1 (APCDD1), a cell-surface lipid-binding protein

Journal Article · 07 May 2023 · Proceedings of the National Academy of Sciences of the United States of America

DOI: https://doi.org/10.1073/pnas.2217096120 · OSTI ID:1972877

Hsieh, Fu-Lien ^[1];

^[1];

^[2];

^[3]

Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD 21205, HHMI, Johns Hopkins University School of Medicine, Baltimore, MD 21205
Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, Department of Medicine, Johns Hopkins University School of Medicine, Baltimore, MD 21205, Department of Oncology, Johns Hopkins University School of Medicine, Baltimore, MD 21205
Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD 21205, HHMI, Johns Hopkins University School of Medicine, Baltimore, MD 21205, Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, MD 21205, Wilmer Eye Institute, Johns Hopkins University School of Medicine, Baltimore, MD 21205

Diverse extracellular proteins negatively regulate WNT signaling. One such regulator is adenomatosis polyposis coli down-regulated 1 (APCDD1), a conserved single-span transmembrane protein. In response to WNT signaling in a variety of tissues, APCDD1 transcripts are highly up-regulated. We have determined the three-dimensional structure of the extracellular domain of APCDD1, and this structure reveals an unusual architecture consisting of two closely apposed β-barrel domains (ABD1 and ABD2). ABD2, but not ABD1, has a large hydrophobic pocket that accommodates a bound lipid. The APCDD1 ECD can also bind to WNT7A, presumably via its covalently bound palmitoleate, a modification that is common to all WNTs and is essential for signaling. This work suggests that APCDD1 functions as a negative feedback regulator by titrating WNT ligands at the surface of responding cells.

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Research Organization:: Brookhaven National Laboratory (BNL), Upton, NY (United States). National Synchrotron Light Source II (NSLS-II)

Sponsoring Organization:: Human Science Frontier Program Organization Fellowship; National Institutes of Health (NIH); USDOE; USDOE Office of Science (SC), Basic Energy Sciences (BES); USDOE Office of Science (SC), Biological and Environmental Research (BER)

Grant/Contract Number:: SC0012704

OSTI ID:: 1972877

Journal Information:: Proceedings of the National Academy of Sciences of the United States of America, Journal Name: Proceedings of the National Academy of Sciences of the United States of America Journal Issue: 20 Vol. 120; ISSN 0027-8424

Publisher:: Proceedings of the National Academy of SciencesCopyright Statement

Country of Publication:: United States

Language:: English

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59 BASIC BIOLOGICAL SCIENCES
WNT signaling
X-ray structure
biological sciences
biophysics and computational biology
extracellular domain
lipid-binding protein
negative feedback regulation
science & technology

Title: Structure of WNT inhibitor adenomatosis polyposis coli down-regulated 1 (APCDD1), a cell-surface lipid-binding protein

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