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2021-09-15

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cc-by (c) Fort i Baixeras, Joana et al., 2021
Please use this identifier to cite or link to this item: https://hdl.handle.net/2445/184216

The Ectodomains of rBAT and 4F2hc Are Fake or Orphan α-Glucosidases

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https://doi.org/10.3390/molecules26206231

Abstract

It is known that 4F2hc and rBAT are the heavy subunits of the heteromeric amino acid transporters (HATs). These heavy subunits are N-glycosylated proteins, with an N-terminal domain, one transmembrane domain and a bulky extracellular domain (ectodomain) that belongs to the α-amylase family. The heavy subunits are covalently linked to a light subunit from the SLC7 family, which is responsible for the amino acid transport activity, forming a heterodimer. The functions of 4F2hc and rBAT are related mainly to the stability and trafficking of the HATs in the plasma membrane of vertebrates, where they exert the transport activity. Moreover, 4F2hc is a modulator of integrin signaling, has a role in cell fusion and it is overexpressed in some types of cancers. On the other hand, some mutations in rBAT are found to cause the malfunctioning of the b0,+ transport system, leading to cystinuria. The ectodomains of 4F2hc and rBAT share both sequence and structure homology with α-amylase family members. Very recently, cryo-EM has revealed the structure of several HATs, including the ectodomains of rBAT and 4F2hc. Here, we analyze available data on the ectodomains of rBAT and 4Fhc and their relationship with the α-amylase family. The physiological relevance of this relationship remains largely unknown. Keywords: N-glycosylation; SLC3; alpha-amylase; alpha-glucosidase; ancillary protein; ectodomain; scaffold protein; structure; transporter.

Subject

Proteïnes portadores, Proteïnes de membrana

Subject (English)

Carrier proteins, Membrane proteins

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Articles publicats en revistes (Bioquímica i Biomedicina Molecular)

Citation

FORT I BAIXERAS, Joana, NICOLÀS-ARAGÓ, Adrià and PALACÍN PRIETO, Manuel. The Ectodomains of rBAT and 4F2hc Are Fake or Orphan α-Glucosidases. Molecules. 2021. Vol. 26, num. 20, pags. 1-13. ISSN 1420-3049. [consulted: 15 of August of 2026]. Available at: https://hdl.handle.net/2445/184216

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