Fungal myosin-1 homologs as key molecular motors at the membrane-cytoskeleton interface

被引:1
|
作者
Tan, Qin-Rong [1 ,2 ]
LI, Xiang-dong [1 ,2 ,3 ]
机构
[1] Chinese Acad Sci, Inst Zool, State Key Lab Integrated Management Insect Pests &, Grp Cell Motil & Muscle Contract, Beijing 100101, Peoples R China
[2] Univ Chinese Acad Sci, Beijing 100049, Peoples R China
[3] Chinese Acad Sci, Inst Zool, Beijing 100101, Peoples R China
基金
中国国家自然科学基金;
关键词
Actin; Cytoskeleton; Endocytosis; Endoplasmic reticulum remodeling; Hyphal growth; Myosin; ARP2/3; COMPLEX; ACANTHAMOEBA MYOSIN; FISSION YEAST; BLEBBISTATIN INHIBITION; MEDIATED ENDOCYTOSIS; CRYSTAL-STRUCTURE; ACTIN NUCLEATION; BINDING SITE; LOCALIZATION; CALMODULIN;
D O I
10.1016/j.fbr.2023.100318
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Class I myosin (myosin-1) is a small, single-headed myosin, distributing from lower eu-karyotes (such as fungi) to higher eukaryotes (such as vertebrates). Being able to interact with actin via the motor domain and to bind to membrane via the tail domain, myosin-1 plays a number of fundamental functions at the membrane-cytoskeleton interface. In fungi, myosin-1 is essential for many cellular processes, including endocytosis, hyphal growth, endoplasmic reticulum (ER) remodeling, and pathogenicity. In this review, we summarize the recent progress of fungal myosin-1 research in the past few years. We first introduce basic structure and function of each fungal myosin-1 domains, then compare the recently solved three-dimensional structure of fungal myosin-1 with that of vertebrate myosin-1, and finally focus on how fungal myosin-1 might participate in endocytosis and ER remodeling.(c) 2023 British Mycological Society. Published by Elsevier Ltd. All rights reserved.
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页数:9
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