FXYD2 Membrane Protein Introduction

Introduction of FXYD2

FXYD2 belongs to the FXYD family, the members of which share a common signature sequences encompassing the transmembrane domain and adjacent regions. FXYD2 is encoded by the FXYD2 gene which is located at 11q23. And the gene mutations can cause hypomagnesemia 2 (HOMG2). Moreover, FXYD2 is a single-pass type III membrane protein, with its N-terminus on the extracellular side of the membrane and no signal sequence.

Function of FXYD2 Membrane Protein

FXYD2 mainly acts as a γ subunit of Na⁺, K⁺-ATPase (NKA) which is required to generate the resting membrane potential in neurons. Association of FXYD2 with α1NKA can negatively regulate the NKA activity by depolarizing the membrane potential of nociceptive neurons. Moreover, the regulation is tissue- and isoform-specific. FXYD2 is found to be expressed in the distal convoluted tubule of kidney and can also be found on basolateral membranes of nephron epithelial cells. FXYD2 plays a role in ATP hydrolysis coupled transmembrane transport, potassium ion import across plasma membrane, regulation of cell growth and proliferation and many other biological processes. Accordingly, the increased FXYD2 activity may be a fundamental mechanism underlying the persistent hypersensitivity to pain induced by inflammation. Beyond that, FXYD1 is highly and specifically expressed in clinical ovarian clear cell carcinoma (OCCC) tissues. It is functionally upregulated in OCCC and likely to be a promising prognostic biomarker and therapeutic target of cardiac glycosides in OCCC. What’ s more, FXYD2 regulates Aδ- and C-fiber mechanosensitivity and is required for the maintenance of neuropathic pain.

Fig.1 Structure of FXYD2b determined in micelles (Gong, 2014).

Application of FXYD2 Membrane Protein in Literature

1. Hsu I.L., et al. Targeting FXYD2 by cardiac glycosides potently blocks tumor growth in ovarian clear cell carcinoma. Oncotarget. 2016, 7(39):62925-62938. PubMed ID: 26910837
   
   

   Authors find that FXYDD2 is highly and specifically expressed in clinical OCCC tissues. They reveal that FXYD2 is functionally upregulated in Ovarian clear cell carcinoma (OCCC) and may serve as a promising prognostic biomarker and therapeutic target of cardiac glycosides in OCCC.

2. Arystarkhova E., Beneficial Renal and Pancreatic Phenotypes in a Mouse Deficient in FXYD2 Regulatory Subunit of Na, K-ATPase. Frontiers in Physiology. 2016, 7. PubMed ID: 27014088
   
   

   This review discuses about functional properties of FXYD2, and unexpected and noteworthy phenotypes discovered in a FXYD2−∕− mouse. FXYD2 modulates both ion transport and signaling.

3. Ventéo S., et al. Fxyd2 regulates Aδ- and C-fiber mechanosensitivity and is required for the maintenance of neuropathic pain. Sci Rep. 2016, 6:36407. PubMed ID: 27805035
   
   

   This article suggests that FXYD2 is specifically required for setting the mechanosensitivity of Aδ-fiber sub-populations of C-fiber nociceptors and low-threshold mechanoreceptors. FXYD2 may function as a potentially promising therapeutic target for peripheral neuropathic pain management.

4. Wang F., et al. FXYD2, a γ subunit of Na⁺, K⁺-ATPase, maintains persistent mechanical allodynia induced by inflammation. Cell Research. 2015, 25(3):318-334. PubMed ID: 25633594
   
   

   This article reveals that FXYD2 is necessary for maintaining the mechanical allodynia induced by peripheral inflammation in nociceptive neurons. The increased FXYD2 activity may be a fundamental mechanism underlying the persistent hypersensitivity to pain induced by inflammation.

5. Burtea C., et al. Development of a peptide-functionalized imaging nanoprobe for the targeting of (FXYD2) γa as a highly specific biomarker of pancreatic beta cells. Contrast Media & Molecular Imaging. 2015, 10(5):398-412. PubMed ID: 25930968
   
   

   This article describes a phage display-derived peptide (P88) that is highly specific to (FXYD2) γa expressed by human beta cells and is proposed to be a molecular vector for the development of functionalized imaging probes.

FXYD2 Preparation Options

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Reference

1. Gong X. M., et al. (2014). Structure of the Na, K-ATPase regulatory protein fxyd2b in micelles: implications for membrane-water interfacial arginines. Biochimica et biophysica acta. 1848(1), 299-306.

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