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相关概念视频

Protein Import into the Peroxisomes01:27

Protein Import into the Peroxisomes

Cells contain membrane-bound organelles called peroxisomes that oxidize organic molecules by transferring hydrogen atoms to oxygen, producing hydrogen peroxide. Peroxisomes enzymatically convert the released hydrogen peroxide into water and oxygen.
Peroxisomal Protein Import:
Peroxisomes lack the genetic machinery required to code for their own proteins. Hence, most peroxisomal membrane, lumenal and transmembrane proteins are synthesized in the cytoplasm or ER and transported to the peroxisome...
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the translocon complex.
Signal Sequences and Sorting Receptors01:41

Signal Sequences and Sorting Receptors

Signal sequences are short amino acid sequences that guide newly synthesized proteins to their proper location within the cell. Classical signal sequences are fifteen to sixty amino acids long and present at the N-terminus of a polypeptide chain. Each signal sequence has a conserved segment of basic residues towards their N terminus, a hydrophobic core, and a C-terminus rich in polar residues. The C-terminus also contains a signal cleavage site and features a -3 -1 sequence motif. The -3-1...
Insertion of Single-pass Transmembrane Proteins in the RER01:26

Insertion of Single-pass Transmembrane Proteins in the RER

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...
Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...

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相关实验视频

Updated: Jun 15, 2026

Translating Extracellular Electron Transfer Activities with Organic Electrochemical Transistors
10:44

Translating Extracellular Electron Transfer Activities with Organic Electrochemical Transistors

Published on: January 31, 2025

人类氧体向信号受体Pex5p被转移到氧体矩阵中并回收到细胞质中.

V Dammai1, S Subramani

  • 1Section of Molecular Biology, Division of Biology, Room 3230 Bonner Hall, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093, USA.

Cell
|May 5, 2001
PubMed
概括

过氧体向信号 (PTS) 受体 Pex5p 在细胞质和过氧体矩阵之间穿. 这种多循环进口机制对于氧体蛋白向至关重要,类似于核进口.

科学领域:

  • 细胞生物学 细胞生物学
  • 分子生物学分子生物学
  • 机体生物学 机体生物学

背景情况:

  • 过氧体向信号 (PTSs) 介导蛋白质进口到过氧体.
  • 细胞质受体 Pex5p 和 Pex7p 识别了 PTS.
  • 氧体膜上的PTS受体在相互作用后的命运在很大程度上是未知的.

研究的目的:

  • 调查货物交付后PTS1受体Pex5p的命运和机制.
  • 为了确定Pex5p在过氧体进口后是否经历回收或降解.

主要方法:

  • 利用了新的实验方法.
  • 采用多种生物化学和成像技术.
  • 专注于人类Pex5p与氧体膜复合物的相互作用.

主要成果:

  • 人类Pex5p参与了多个进口循环进入过氧体矩阵.
  • 在矩阵进入后,Pex5p独立于PTS2通路,被输出回细胞质.
  • 这表明了PTS1受体的独特穿机制.

结论:

  • 过氧体蛋白质进口涉及一个动态穿Pex5p受体.

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Introduction to Solid Supported Membrane Based Electrophysiology
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Proteomics to Identify Proteins Interacting with P2X2 Ligand-Gated Cation Channels

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相关实验视频

Last Updated: Jun 15, 2026

Translating Extracellular Electron Transfer Activities with Organic Electrochemical Transistors
10:44

Translating Extracellular Electron Transfer Activities with Organic Electrochemical Transistors

Published on: January 31, 2025

Introduction to Solid Supported Membrane Based Electrophysiology
19:56

Introduction to Solid Supported Membrane Based Electrophysiology

Published on: May 11, 2013

Proteomics to Identify Proteins Interacting with P2X2 Ligand-Gated Cation Channels
16:36

Proteomics to Identify Proteins Interacting with P2X2 Ligand-Gated Cation Channels

Published on: May 19, 2009

  • 这种机制使氧体进口与大多数其他有机体区分开来,类似于核进口通路.