SERINC3 Membrane Protein Introduction

Introduction of SERINC3

Serine incorporator 3 encoded by SERINC3 gene is described as a carrier protein that incorporates a polar-amino acid serine into cell membranes. It is a member of the serine incorporator (SERINC) protein family that is conserved from yeast to mammals. The members of this family share between 30 and 80% homology, contain multiple hydrophobic domains and often include an N-terminal signal peptide. In mouse, at least five homologues have been identified, scattered over four different chromosomes, whereas human SERINC3 genes have been found on five different chromosomes. When comparing the sequence between human and mouse genes, it has been noted that most homologues between these two species locate on syntenic regions at the chromosome level suggesting evolutionary conservation. The conserved nature of the gene structure and of the sequence of the protein through evolution suggests an important biological role for SERINC family members.

Function of SERINC3 Membrane Protein

SERINC protein function has not been studied in great detail and essentially relies on a small number of reports. SERINC3 and SERINC5 together restrict HIV-1 replication, and this restriction is evaded by Nef. Moreover, SERINC3 and SERINC5 are highly expressed in primary human HIV-1 target cells, which may suggest a potential strategy to combat HIV. Except for that function, human SERINC5 overexpression can be observed in tumor tissues of tumor-bearing transgenic mice. However, the ultimate role of SERINC5 in human cell transformation, and specifically, its possible role in human carcinogenesis, needs to be further investigated. The present study also underlies the ability of SERINC5 to interfere with programmed cell death, allowing cells to escape control mechanisms established in multicellular organisms to eliminate malfunctioning cells such as transformed cells.

Fig.1 Cytoplasmic host cell restrictions to human immunodeficiency virus types 1 (HIV-1) infection and virally encoded antagonists. (Fackler, 2015)

Application of SERINC3 Membrane Protein in Literature

1. Usami Y., et al. SERINC3 and SERINC5 restrict HIV-1 infectivity and are counteracted by Nef. Nature. 2015, 526(7572):218-23. PubMed ID: 26416733
   
   

   This article finds that HIV-1 Nef and MLV glycoGag efficiently down-regulate SERINC3 and SERINC5 form the cell surface, which prevents their incorporation into HIV-1 virions and consequently counteracts their inhibitory effect on HIV-1 infectivity.

2. Fackler O.T. Spotlight on HIV-1 Nef: SERINC3 and SERINC5 identified as restriction factors antagonized by the pathogenesis factor. Viruses. 2015, 7(12):6730-8. PubMed ID: 26703715
   
   

   This article establishes SERINC3/5 as restrictions to HIV replication in human cells and defines a novel activity for the HIV pathogenesis factor Nef.

3. Murrell B., et al. The evolutionary histories of antiretroviral proteins SERINC3 and SERINC5 do not support an evolutionary arms race in primates. Journal of Virology. 2016, 90(18):8085-9. PubMed ID: 27356902
   
   

   This article suggests that the importance of the antiretroviral function of the SERINC proteins may be a relatively novel evolutionary advance.

4. Chande A., et al. S2 from equine infectious anemia virus is an infectivity factor which counteracts the retroviral inhibitors SERINC5 and SERINC3. Proc Natl Acad Sci USA. 2016, 113(46):13197-13202. PubMed ID: 27803322
   
   

   This article reveals that SERINC5 and SERINC3 play an essential role against various retrovirus pathogens.

5. Bossolasco M., et al. Human TDE1, a TDE1/TMS family member, inhibits apoptosis in vitro and stimulates in vivo tumorigenesis. Oncogene. 2006, 25(33):4549-58. PubMed ID: 16547497
   
   

   This article suggests that human TDE1 contributes directly to oncogenesis in vivo.

SERINC3 Preparation Options

Membrane protein studies have applied in many fields. Based on our versatile Magic™ membrane protein production platform, we could offer a series of membrane protein preparation services for worldwide customers in reconstitution forms as well as multiple active formats. Besides, aided by our versatile Magic™ anti-membrane protein antibody discovery platform, we also provide customized anti-SERINC3 antibody development services.

• Magic™ Membrane Protein Production Platform
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During the past years, Creative Biolabs has successfully generated many functional membrane proteins for our global customers. We are happy to accelerate the development of our clients’ programs with our one-stop, custom-oriented service. For more detailed information, please feel free to contact us.

Reference

1. Fackler O T. (2015). Spotlight on HIV-1 Nef: SERINC3 and SERINC5 identified as restriction factors antagonized by the pathogenesis factor. Viruses. 7(12), 6730-8.

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