FAM53B

Last update 23 Jan 2025

Basic Info

Synonyms

bA12J10.2, FAM53B, family with sequence similarity 53 member B

+ [4]

Introduction

Acts as a regulator of Wnt signaling pathway by regulating beta-catenin (CTNNB1) nuclear localization.

100 Clinical Results associated with FAM53B

100 Translational Medicine associated with FAM53B

0 Patents (Medical) associated with FAM53B

302

Literatures (Medical) associated with FAM53B

01 Jan 2025·Plant, Cell & Environment

Functional and Structural Analysis Reveals Distinct Biological Roles of Plant Synaptotagmins in Response to Environmental Stress

Article

Author: Rivera‐Moreno, María ; Morello‐López, Jorge ; García‐Hernández, Selene ; Pérez‐Sancho, Jessica ; Rubio, Lourdes ; Benítez‐Fuente, Francisco ; Albert, Armando ; Beuzón, Carmen R. ; Ruiz‐López, Noemi ; Esteban del Valle, Alicia ; Botella, Miguel A. ; Macho, Alberto P.

ABSTRACTEndoplasmic reticulum–plasma membrane contact sites (ER–PM CSs) are evolutionarily conserved membrane domains found in all eukaryotes, where the ER closely interfaces with the PM. This short distance is achieved in plants through the action of tether proteins such as synaptotagmins (SYTs). Arabidopsis comprises five SYT members (SYT1–SYT5), but whether they possess overlapping or distinct biological functions remains elusive. SYT1, the best‐characterized member, plays an essential role in the resistance to abiotic stress. This study reveals that the functionally redundant SYT1 and SYT3 genes, but not SYT5, are involved in salt and cold stress resistance. We also show that, unlike SYT5, SYT1 and SYT3 are not required for Pseudomonas syringae resistance. Since SYT1 and SYT5 interact in vivo via their SMP domains, the distinct functions of these proteins cannot be caused by differences in their localization. Interestingly, structural phylogenetic analysis indicates that the SYT1 and SYT5 clades emerged early in the evolution of land plants. We also show that the SYT1 and SYT5 clades exhibit different structural features in their SMP and Ca2+ binding of their C2 domains, rationalizing their distinct biological roles.

01 Jan 2025·Methods in Molecular Biology

DNA-Assisted Assays for Studying Lipid Transfer Between Membranes

Article

Author: Bian, Xin ; Wang, Yunyun ; Yang, Yang ; Yang, Qiulan ; Shi, Qian

Extended-synaptotagmins (E-Syts) are proteins located on the endoplasmic reticulum (ER) that tether the ER to the plasma membrane (PM) and regulate their lipid homeostasis via its lipid transfer module, the synaptotagmin-like mitochondrial lipid-binding protein (SMP) domain. Here, we describe in vitro DNA nanostructure-assisted lipid transfer assays investigating how the SMP domain transports lipids between membranes and associates with the membranes to extract and release lipids. The lipid transfer signal was detected through fluorescence resonance energy transfer (FRET). This method overcomes the limitations of commonly used lipid transfer assays in accurately controlling inter-liposome distance and liposome size, enabling us to further understand the details involved in the process of SMP domain-mediated lipid transfer. Similar platforms can be extended to studying the lipid transfer distance and membrane curvature sensitivity of other lipid transfer proteins.

01 Dec 2024·Biochimie

Specificity of lipid transfer proteins: An in vitro story

Review

Author: Drin, Guillaume ; Hamaï, Amazigh

Lipids, which are highly diverse, are finely distributed between organelle membranes and the plasma membrane (PM) of eukaryotic cells. As a result, each compartment has its own lipid composition and molecular identity, which is essential for the functional fate of many proteins. This distribution of lipids depends on two main processes: lipid synthesis, which takes place in different subcellular regions, and the transfer of these lipids between and across membranes. This review will discuss the proteins that carry lipids throughout the cytosol, called LTPs (Lipid Transfer Proteins). More than the modes of action or biological roles of these proteins, we will focus on the in vitro strategies employed during the last 60 years to address a critical question: What are the lipid ligands of these LTPs? We will describe the extent to which these strategies, combined with structural data and investigations in cells, have made it possible to discover proteins, namely ORPs, Sec14, PITPs, STARDs, Ups/PRELIs, START-like, SMP-domain containing proteins, and bridge-like LTPs, which compose some of the main eukaryotic LTP families, and their lipid ligands. We will see how these approaches have played a central role in cell biology, showing that LTPs can connect distant metabolic branches, modulate the composition of cell membranes, and even create new subcellular compartments.

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FAM53B

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