癌症中的跨膜蛋白:从机制到临床影响的见解
Chih-Wen Shu1,2,3, Chia-Hsuan Chang1, Hsing-Hsiang Wang3
1Institute of BioPharmaceutical Sciences, National Sun Yat-sen University, Kaohsiung80424, Taiwan.
Open biology
|February 4, 2026
概括
跨膜蛋白 (TMEMs) 对于细胞功能至关重要,并与癌症有关. 本综述将TMEM分类为致癌性,瘤抑制性或双重功能,强调其在癌症发展和治疗潜力的作用.
科学领域:
- 分子生物学分子生物学
- 在瘤学瘤学.
- 生物化学 生物化学
背景情况:
- 跨膜蛋白 (TMEMs) 对于细胞平衡至关重要.
- TMEMs的失调越来越多地与癌症的发展和进展有关.
- 了解TMEM在癌症中的作用对于治疗进步至关重要.
研究的目的:
- 审查TMEM在癌症中的多方面的作用.
- 根据其致癌性,瘤抑制性或双重功能对TMEM进行分类.
- 要总结涉及各种癌症类型及其相关途径的已知TMEM.
主要方法:
- 文献审查和数据库选.
- 基于TMEM在癌症中的功能作用的分类.
- 在不同类型的癌症中,TMEMs的参与概述.
主要成果:
- TMEMs可以作为瘤基因或瘤抑制剂.
- 识别了具有瘤,瘤抑制和双重功能的TMEM.
- 突出的TMEM,包括那些有不清楚的机制和相关的信号通路的TMEM.
结论:
- TMEM在癌症病原发生过程中起着至关重要的作用.
- 对TMEM机制,预后价值和治疗向的进一步研究是有必要的.
- TMEMs代表了新型癌症治疗的有希望的目标.
相关概念视频
Single-pass Transmembrane Proteins
6.7K
Integral membrane proteins are tightly associated with the cell membrane and play a crucial role in cell communication, signaling, adhesion, and transport of the molecules. Some integral membrane proteins are present only in the membrane monolayer. For example, the enzyme fatty acid amide hydrolase is present in the cytoplasmic side of the membrane monolayer. In contrast, another type of integral membrane protein, also known as a transmembrane protein, spans across the membrane. Transmembrane...
6.7K
Mechanical Protein Functions
5.6K
Proteins perform many mechanical functions in a cell. These proteins can be classified into two general categories- proteins that generate mechanical forces and proteins that are subjected to mechanical forces. Proteins providing mechanical support to the structure of the cell, such as keratin, are subjected to mechanical force, whereas proteins involved in cell movement and transport of molecules across cell membranes, such as an ion pump, are examples of generating mechanical force.
5.6K
Insertion of Single-pass Transmembrane Proteins in the RER
18.1K
Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
18.1K
Insertion of Multi-pass Transmembrane Proteins in the RER
18.4K
The rough ER membrane synthesizes, assembles, and embeds transmembrane proteins in diverse topologies. These proteins function as transporters or channels and can remain in the ER membrane or are sent to the Golgi complex, lysosome, and cell membrane.
The multipass transmembrane proteins are the type IV integral membrane proteins with multiple topogenic sequences determining their spatial arrangement in the ER membrane. Nearly all multipass proteins lack a cleavable signal sequence and use...
The multipass transmembrane proteins are the type IV integral membrane proteins with multiple topogenic sequences determining their spatial arrangement in the ER membrane. Nearly all multipass proteins lack a cleavable signal sequence and use...
18.4K
Multi-pass Transmembrane Proteins and β-barrels
6.6K
In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as...
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as...
6.6K
Mechanical Protein Function
2.5K
2.5K


