Early eukaryotic origins and metazoan elaboration of MAPR family proteins

Hehenberger, Elisabeth, Eitel, Michael, Fortunato, Sofia A.V., Miller, David J., Keeling, Patrick J., and Cahill, Michael A. (2020) Early eukaryotic origins and metazoan elaboration of MAPR family proteins. Molecular Phylogenetics and Evolution, 148. 106814.

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Abstract

The membrane-associated progesterone receptor (MAPR) family consists of heme-binding proteins containing a cytochrome b5 (cytb5) domain characterized by the presence of a MAPR-specific interhelical insert region (MIHIR) between helices 3 and 4 of the canonical cytb5-domain fold. Animals possess three MAPR genes (PGRMC-like, Neuferricin and Neudesin). Here we show that all three animal MAPR genes were already present in the common ancestor of the opisthokonts (comprising animals and fungi as well as related single-celled taxa). All three MAPR genes acquired extensions C-terminal to the cytb5 domain, either before or with the evolution of animals. The archetypical MAPR protein, progesterone receptor membrane component 1 (PGRMC1), contains phosphorylated tyrosines Y139 and Y180. The combination of Y139/Y180 appeared in the common ancestor of cnidarians and bilaterians, along with an early embryological organizer and synapsed neurons, and is strongly conserved in all bilaterian animals. A predicted protein interaction motif in the PGRMC1 MIHIR is potentially regulated by Y139 phosphorylation. A multilayered model of animal MAPR function acquisition includes some pre-metazoan functions (e.g., heme binding and cytochrome P450 interactions) and some acquired animal-specific functions that involve regulation of strongly conserved protein interaction motifs acquired by animals (Metazoa). This study provides a conceptual framework for future studies, against which especially PGRMC1′s multiple functions can perhaps be stratified and functionally dissected.

Item ID: 64233
Item Type: Article (Research - C1)
ISSN: 1095-9513
Keywords: Membrane-associated progesterone receptor, Multicellularity, Phylogeny, Organizer, Opisthokont, Protein evolution, Tyrosine phosphorylation, Holozoa
Copyright Information: © 2020 Elsevier Inc. All rights reserved.
Funders: Charles Sturt University (CSU)
Projects and Grants: CSU School of Biomedical Sciences (SBMS) Compact grant A541-900-xxx-40513, CSU School of Biomedical Sciences (SBMS) Support A534-900-xxx-41066, CSU Competitive grant A102-900-xxx-40002
Date Deposited: 02 Sep 2020 07:33
FoR Codes: 31 BIOLOGICAL SCIENCES > 3104 Evolutionary biology > 310401 Animal systematics and taxonomy @ 100%
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