Literature DB >> 35713844

Mechanisms of PiT2-loop7 Missense Mutations Induced Pi Dyshomeostasis.

Hao Sun1, Xuan Xu2, Junyu Luo1, Tingbin Ma2, Jiaming Cui2, Mugen Liu1, Bo Xiong3, Shujia Zhu4, Jing-Yu Liu5.   

Abstract

PiT2 is an inorganic phosphate (Pi) transporter whose mutations are linked to primary familial brain calcification (PFBC). PiT2 mainly consists of two ProDom (PD) domains and a large intracellular loop region (loop7). The PD domains are crucial for the Pi transport, but the role of PiT2-loop7 remains unclear. In PFBC patients, mutations in PiT2-loop7 are mainly nonsense or frameshift mutations that probably cause PFBC due to C-PD1131 deletion. To date, six missense mutations have been identified in PiT2-loop7; however, the mechanisms by which these mutations cause PFBC are poorly understood. Here, we found that the p.T390A and p.S434W mutations in PiT2-loop7 decreased the Pi transport activity and cell surface levels of PiT2. Furthermore, we showed that these two mutations attenuated its membrane localization by affecting adenosine monophosphate-activated protein kinase (AMPK)- or protein kinase B (AKT)-mediated PiT2 phosphorylation. In contrast, the p.S121C and p.S601W mutations in the PD domains did not affect PiT2 phosphorylation but rather impaired its substrate-binding abilities. These results suggested that missense mutations in PiT2-loop7 can cause Pi dyshomeostasis by affecting the phosphorylation-regulated cell-surface localization of PiT2. This study helps understand the pathogenesis of PFBC caused by PiT2-loop7 missense mutations and indicates that increasing the phosphorylation levels of PiT2-loop7 could be a promising strategy for developing PFBC therapies.
© 2022. Center for Excellence in Brain Science and Intelligence Technology, Chinese Academy of Sciences.

Entities:  

Keywords:  Mutation; Phosphorylation; Pi dyshomeostasis; PiT2-loop7; Primary familial brain calcification

Year:  2022        PMID: 35713844     DOI: 10.1007/s12264-022-00893-y

Source DB:  PubMed          Journal:  Neurosci Bull        ISSN: 1995-8218            Impact factor:   5.203


  45 in total

1.  Transmembrane topology of PiT-2, a phosphate transporter-retrovirus receptor.

Authors:  C Salaün; P Rodrigues; J M Heard
Journal:  J Virol       Date:  2001-06       Impact factor: 5.103

Review 2.  Proximal tubular phosphate reabsorption: molecular mechanisms.

Authors:  H Murer; N Hernando; I Forster; J Biber
Journal:  Physiol Rev       Date:  2000-10       Impact factor: 37.312

3.  Cloning of the cellular receptor for amphotropic murine retroviruses reveals homology to that for gibbon ape leukemia virus.

Authors:  D G Miller; R H Edwards; A D Miller
Journal:  Proc Natl Acad Sci U S A       Date:  1994-01-04       Impact factor: 11.205

4.  Mutations in SLC20A2 link familial idiopathic basal ganglia calcification with phosphate homeostasis.

Authors:  Cheng Wang; Yulei Li; Lei Shi; Jie Ren; Monica Patti; Tao Wang; João R M de Oliveira; María-Jesús Sobrido; Beatriz Quintáns; Miguel Baquero; Xiaoniu Cui; Xiang-Yang Zhang; Lianqing Wang; Haibo Xu; Junhan Wang; Jing Yao; Xiaohua Dai; Juan Liu; Lu Zhang; Hongying Ma; Yong Gao; Xixiang Ma; Shenglei Feng; Mugen Liu; Qing K Wang; Ian C Forster; Xue Zhang; Jing-Yu Liu
Journal:  Nat Genet       Date:  2012-02-12       Impact factor: 38.330

5.  Cell-surface receptors for gibbon ape leukemia virus and amphotropic murine retrovirus are inducible sodium-dependent phosphate symporters.

Authors:  M P Kavanaugh; D G Miller; W Zhang; W Law; S L Kozak; D Kabat; A D Miller
Journal:  Proc Natl Acad Sci U S A       Date:  1994-07-19       Impact factor: 11.205

Review 6.  The SLC20 family of proteins: dual functions as sodium-phosphate cotransporters and viral receptors.

Authors:  James F Collins; Liqun Bai; Fayez K Ghishan
Journal:  Pflugers Arch       Date:  2003-05-21       Impact factor: 3.657

7.  The cellular receptor for gibbon ape leukemia virus is a novel high affinity sodium-dependent phosphate transporter.

Authors:  Z Olah; C Lehel; W B Anderson; M V Eiden; C A Wilson
Journal:  J Biol Chem       Date:  1994-10-14       Impact factor: 5.157

8.  The central half of Pit2 is not required for its function as a retroviral receptor.

Authors:  Pernille Bøttger; Lene Pedersen
Journal:  J Virol       Date:  2004-09       Impact factor: 5.103

9.  Chimeras of receptors for gibbon ape leukemia virus/feline leukemia virus B and amphotropic murine leukemia virus reveal different modes of receptor recognition by retrovirus.

Authors:  L Pedersen; S V Johann; M van Zeijl; F S Pedersen; B O'Hara
Journal:  J Virol       Date:  1995-04       Impact factor: 5.103

10.  Mapping of the minimal inorganic phosphate transporting unit of human PiT2 suggests a structure universal to PiT-related proteins from all kingdoms of life.

Authors:  Pernille Bøttger; Lene Pedersen
Journal:  BMC Biochem       Date:  2011-05-17       Impact factor: 4.059

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