SLC39A13 Membrane Protein Introduction

Introduction of SLC39A13

Based on amino acid sequence similarity, the ZIP family was divided into four subfamilies: ZIPI, ZIPII, GufA, and LZT. SCL39A13 belongs to the LZT family, the members of which share the Pro-Ala-Leu (PAL) and His-Glu-X-X-His (HEXXH) motifs. The conserved PAL motif is in the N-terminal region and may be involved in protein processing. The HEXXH motif is located within the TM5 region. However, SLC39A13 also possesses some domains that are not found in other LZT family members. SLC39A13 is mainly expressed and functions in mesenchyme-originating cells. Moreover, it is localized to the Golgi apparatus and intracellular vesicles. ZIP13 has a putative 8 membrane-spanning segments and the N terminus and C terminus of this protein facing the luminal side.

Functions of SLC39A13 Membrane Protein

As a member of the SLC39 family, SLC39A13 mediates Zn²⁺ influx. The zinc transporter protein SLC39A13 plays critical roles in bone, tooth, and connective tissue development. Dysfunction of the SLC39A13 transporter can lead to a genetic disorder of connective tissues, bones, and teeth, which is named the spondylocheiro dysplastic form of Ehlers-Danlos syndrome (SCD-EDS). Patients with this genetic disorder show short stature, skeletal dysplasia of the spine, and clinical abnormalities of the hands and teeth, in addition to the common features of EDS such as skin and joint looseness.

Fig.1 The predicted topology model of ZIP13. (Kambe,2014)

Application of SLC39A13 Membrane Protein in Literature

1. Bin B.H., et al. Molecular pathogenesis of Spondylocheirodysplastic Ehlers-Danlos syndrome caused by mutant ZIP13 proteins. EMBO molecular medicine. 2014, 6(8): 1028-1042. PubMed ID: 25007800
   
   

   This study investigated the molecular pathogenic mechanism of SCD-EDS caused by two different mutant ZIP13 proteins that were found in human patients, one is the ZIP13(G64D) and the other is ZIP13(ΔFLA). The findings uncovered the pathogenic mechanisms elicited by these two mutant proteins.

2. Xiao G., et al. The metal transporter ZIP13 supplies iron into the secretory pathway in Drosophila melanogaster. Elife. 2014, 3: e03191. PubMed ID:
   
   

   This study identified the ZIP13 proteins as the iron transporter responsible for iron delivery to the secretory compartments.

3. Bin B.H., et al. Biochemical characterization of human ZIP13 protein a homo-dimerized zinc transporter involved in the spondylocheiro dysplastic Ehlers-danlos syndrome. Journal of Biological Chemistry. 2011, 286(46): 40255-40265. PubMed ID: 21917916
   
   

   This study conducted a biochemical characterization of the human ZIP13 protein, which provided important information for further investigations of its structural characteristics and function.

4. Fukunaka A., et al. Zinc transporter ZIP13 suppresses beige adipocyte biogenesis and energy expenditure by regulating C/EBP-β expression. PLoS genetics. 2017, 13(8): e1006950. PubMed ID: 28854265
   
   

   This study investigated the underlying mechanisms of the genetic mutations in ZIP13 leading to reduced adipose tissue mass in humans. The results showed that the ZIP13 suppressed beige adipocyte biogenesis and energy expenditure by regulating C/EBP-β expression. This might contribute significantly to the development of new therapies for obesity and metabolic syndrome.

5. Hirose T., et al. Comparative study of dermal components and plasma TGF-β1 levels in Slc39a13/Zip13-KO mice. Journal of Veterinary Medical Science. 2015, 77(11): 1385-1389. PubMed ID: 26050750
   
   

   This study investigated the characteristics of the dermis of the Zip13-knockout (KO) mouse, an animal model for SCD-EDS. The results suggested that skin fragility due to defective ZIP13 protein may be owing to impaired extracellular matrix synthesis accompanied by abnormal peripheral transforming growth factor-β homeostasis.

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Reference

1. Kambe T, et al. (2014). Current understanding of ZIP and ZnT zinc transporters in human health and diseases. Cellular and molecular life sciences. 71(17): 3281-3295.

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