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Related Concept Videos

Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

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Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
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Translocation of Proteins into the Mitochondria01:19

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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,...
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Protein Transport into the Inner Mitochondrial Membrane01:34

Protein Transport into the Inner Mitochondrial Membrane

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Nuclear encoded mitochondrial precursors are imported to the inner membrane in a multistep process involving two separate translocons, TIM22 and TIM23. TIM23 is a cation-selective pore that remains closed by the N terminal segment of the protein. Negative charges on the TIM23 act as a receptor for the incoming precursor, pulling the positively charged matrix-targeting sequence for peptide insertion and translocation.
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Tail-anchoring of Proteins in the ER Membrane01:45

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Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
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Lipids as Anchors01:32

Lipids as Anchors

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In the plasma membrane, the lipids forming the bilayer can also act as an anchor to tether proteins to the membrane. The three main types of lipid anchors found in eukaryotes are – prenyl groups, fatty acyl groups, and glycosylphosphatidylinositol or GPI groups. Prenyl and fatty acyl groups act as anchors on the cytosolic surface of the membrane, whereas GPI anchors proteins on the extracellular side.
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Membrane Fluidity01:26

Membrane Fluidity

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Membrane fluidity is explained by the fluid mosaic model of the cell membrane, which describes the plasma membrane structure as a mosaic of components—including phospholipids, cholesterol, proteins, and carbohydrates—that gives the membrane a fluid character.
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Related Experiment Video

Updated: Aug 7, 2025

PIP-on-a-chip: A Label-free Study of Protein-phosphoinositide Interactions
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PIP-on-a-chip: A Label-free Study of Protein-phosphoinositide Interactions

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Structural insight into TIPE1 functioning as a lipid transfer protein.

Sujian Cao1,2, Ye Zhang1, Haoqian Jiang3

  • 1Advanced Medical Research Institute, Interventional Medicine Department, The Second Hospital, Cheeloo College of Medicine, Shandong University, Jinan, China.

Journal of Biomolecular Structure & Dynamics
|March 10, 2023
PubMed
Summary
This summary is machine-generated.

Tumor necrosis factor-α-induced protein 8-like 1 (TIPE1) binds phospholipids like phosphatidylethanolamine and phosphatidylinositol. This study reveals TIPE1

Keywords:
G-proteinTIPE1lipid transfer proteinphosphatidylinositoltumor

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Single-molecule Super-resolution Imaging of Phosphatidylinositol 4,5-bisphosphate in the Plasma Membrane with Novel Fluorescent Probes
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Single-molecule Super-resolution Imaging of Phosphatidylinositol 4,5-bisphosphate in the Plasma Membrane with Novel Fluorescent Probes
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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • TIPE1, part of the TNFAIP8/TIPE family, influences apoptosis, autophagy, and tumorigenesis.
  • Its precise role in cellular signaling networks is not fully understood.

Purpose of the Study:

  • To elucidate the structural basis of TIPE1's interactions with phospholipids.
  • To identify and characterize TIPE1's protein-binding partners and their interaction modes.

Main Methods:

  • X-ray crystallography of zebrafish TIPE1 complexed with phosphatidylethanolamine (PE).
  • Molecular dynamics (MD) simulations to study TIPE1-phosphatidylinositol (PI) interactions.
  • GST pull-down assays and size-exclusion chromatography to identify protein partners.
  • Key-residue mutation analyses and complex structure prediction.

Main Results:

  • Determined the crystal structure of zebrafish TIPE1 with PE at 1.38 Å resolution.
  • Proposed a conserved phospholipid-binding mode within the TIPE family.
  • Elucidated the role of the N-terminal domain in phosphatidylinositol (PI) binding via MD simulations.
  • Identified Gαi3 as a direct binding partner of TIPE1.
  • Revealed a potentially non-canonical binding mode between TIPE1 and Gαi3.

Conclusions:

  • Established a universal phospholipid-binding mechanism for TIPE family proteins.
  • Defined TIPE1's interaction with Gαi3 and its role in Gαi3-related signaling.
  • Positioned TIPE1 within phosphatidylinositol (PI)-mediated signaling pathways.