PLEKHF2

Last update 08 May 2025

Basic Info

Synonyms

EAPF, Endoplasmic reticulum-associated apoptosis-involved protein containing PH and FYVE domains, FLJ13187

+ [9]

Introduction

May play a role in early endosome fusion upstream of RAB5, hence regulating receptor trafficking and fluid-phase transport. Enhances cellular sensitivity to TNF-induced apoptosis (PubMed:18288467).

100 Clinical Results associated with PLEKHF2

100 Translational Medicine associated with PLEKHF2

0 Patents (Medical) associated with PLEKHF2

Literatures (Medical) associated with PLEKHF2

01 Nov 2024·Fish & Shellfish Immunology

Two novel antimicrobial peptides P33-57 and mP168-187 from zebrafish showing potent antibacterial activities

Article

Author: He, Jing ; Guo, Dongqiu ; Liu, Longxiao ; Wang, Xia ; Zhang, Liqiao ; Wang, Hao

It is known that overuse or abuse of antibiotics has undoubtedly accelerated the global antibiotic resistance crisis, and long-time use of antibiotics may have adverse effects on the health of animal, human, and ecosystem. Therefore, it is necessary to find antibiotic alternatives that can be used in aquaculture and are non-toxic to the human. Here we clearly demonstrated that both the PH and FYVE domain of Plekhf2 in zebrafish have antibacterial properties and can interact with PGN in this study. Therefore, we screened four candidate peptides from the two domains. It was demonstrated that P_152-172 and P_168-187 had no obvious antibacterial activities, while P_33-57 and mP_168-187 had strong antibacterial activities, which may be used as antimicrobial peptides. Additionally, transmission electron microscopy experiment revealed that P_33-57 and mP_168-187 can destroy the cell wall of bacteria, thereby directly killing bacteria. Importantly, it was found that P_33-57 and mP_168-187 had no hemolysis to red blood cells and lacked cytotoxicity. In summary, P_33-57 and mP_168-187could be seen as antibacterial activity centers of PLEKHF2 and may be promising antimicrobial peptides to combat bacterial infections facing an antibiotic-resistance crisis.

27 Jun 2024·Open Life Sciences

The role of Phafin proteins in cell signaling pathways and diseases

Review

Author: Tang, Tuoxian ; Li, Chen ; Sun, Jing

AbstractMembrane-associated proteins are important membrane readers that mediate and facilitate the signaling and trafficking pathways in eukaryotic membrane-bound compartments. The protein members in the Phafin family are membrane readers containing two phosphoinositide recognition domains: the Pleckstrin Homology domain and the FYVE (Fab1, YOTB, Vac1, and early endosome antigen 1) domain. Phafin proteins, categorized into two subfamilies, Phafin1 and Phafin2, associate with cellular membranes through interactions involving membrane-embedded phosphoinositides and phosphoinositide-binding domains. These membrane-associated Phafin proteins play pivotal roles by recruiting binding partners and forming complexes, which contribute significantly to apoptotic, autophagic, and macropinocytotic pathways. Elevated expression levels of Phafin1 and Phafin2 are observed in various cancers. A recent study highlights a significant increase in Phafin1 protein levels in the lungs of idiopathic pulmonary fibrosis patients compared to normal subjects, suggesting a crucial role for Phafin1 in the pathogenesis of pulmonary fibrosis. Additionally, phosphatidylinositol-3-phosphate-binding 2 (Pib2), a close relative of the Phafin1 protein, functions as an amino acid sensor activating the TOCR1 pathway in yeasts. This review focuses on delineating the involvement of Phafin proteins in cellular signaling and their implications in diseases and briefly discusses the latest research findings concerning Pib2.

01 Aug 2022·Fish & Shellfish Immunology

Identification of zebrafish PLEKHF2 presents in egg/embryos as an antibacterial protein

Article

Author: Wang, Xia ; Wang, Chunqiu ; Chang, Qingqi ; Wang, Hao ; Ren, Yiqing ; Guo, Dongqiu

PLEKHF2 proteins are widespread in animals, but their functions and mechanisms remain poorly defined. Here we clearly demonstrate that PLEKHF2 is a newly identified present abundantly in the eggs/embryos of zebrafish. We also show that recombinant PLEKHF2 acts as a pattern recognition receptor capable of identifying the bacterial signature molecule PGN, LPS, and LTA, binding the bacteria, and functions as an antibacterial effector directly killing the bacteria. In brief, these results indicate that PLEKHF2 is an antibacterial protein, a novel role assigned to PLEKHF2 proteins.

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PLEKHF2

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