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Conservation of Protein Domains Over Different Proteins

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain. Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...

Single-pass Transmembrane Proteins

Single-pass Transmembrane Proteins

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...

Phosphoinositides and PIPs

Phosphoinositides and PIPs

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...

Tail-anchoring of Proteins in the ER Membrane

Tail-anchoring of Proteins in the ER Membrane

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...

Multi-pass Transmembrane Proteins and β-barrels

Multi-pass Transmembrane Proteins and β-barrels

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 G-protein-linked receptors (GPCRs) and...

Structure of Porins

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Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel precursors...

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Related Experiment Video

Updated: Jul 17, 2026

Identification of Post-translational Modifications of Plant Protein Complexes

Identification of Post-translational Modifications of Plant Protein Complexes

Published on: February 22, 2014

The function of PTB domain proteins.

B Margolis¹, J P Borg, S Straight

¹Department of Internal Medicine and Biological Chemistry, Howard HughesMedical Institute, University of Michigan Medical School, Ann Arbor 48109-0650, USA. bmargoli@uv1.im.med.umich.edu

Kidney International

|December 28, 1999

Summary

Phosphotyrosine binding (PTB) domains mediate protein interactions crucial for cell signaling. These domains can bind targets dependently or independently of phosphotyrosine, enabling diverse cellular roles.

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Last Updated: Jul 17, 2026

Identification of Post-translational Modifications of Plant Protein Complexes

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Area of Science:

Molecular Biology
Cell Biology
Biochemistry

Background:

Phosphotyrosine binding (PTB) domains are critical protein modules involved in signal transduction.
PTB domains in proteins like Shc and IRS-1 mediate phosphotyrosine-dependent interactions, essential for growth factor receptor signaling.
However, some PTB domains, such as in the X11 protein family, exhibit phosphotyrosine-independent binding.

Purpose of the Study:

To investigate the dual binding capabilities of PTB domains.
To explore the role of phosphotyrosine-independent PTB domain interactions in protein complex formation and cellular targeting.
To understand the broader implications of PTB domain versatility in cellular functions.

Main Methods:

Bioinformatic analysis of protein domains.
Protein-peptide interaction studies.
Analysis of protein complex formation in model organisms (C. elegans) and mammalian systems.

Main Results:

PTB domains demonstrate both phosphotyrosine-dependent and -independent peptide binding modes.
The X11/Lin-10 PTB domain functions in phosphotyrosine-independent interactions.
X11/Lin-10, along with Lin-2 and Lin-7, forms a complex critical for basolateral protein targeting in C. elegans epithelia.

Conclusions:

The dual binding nature of PTB domains allows for diverse roles in cellular processes.
The X11/Lin-10 protein complex is essential for receptor targeting to the basolateral surface in epithelia.
This protein complex likely plays a conserved role in cell surface protein targeting in both invertebrates and mammals.