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Phosphorylation

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...

Phosphorylation

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...

Regulation of Nuclear Protein Sorting

Regulation of Nuclear Protein Sorting

Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...

Protein Kinases and Phosphatases

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...

Protein Kinases and Phosphatases

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...

Amplifying Signals via Enzymatic Cascade

Amplifying Signals via Enzymatic Cascade

When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze the...

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Assessing Cellular Target Engagement by SHP2 (PTPN11) Phosphatase Inhibitors

Assessing Cellular Target Engagement by SHP2 (PTPN11) Phosphatase Inhibitors

Published on: July 17, 2020

Phosphorylation controls a dual-function polybasic nuclear localization sequence in the adapter protein SH2B1β to

Travis J Maures¹, Hsiao-Wen Su, Lawrence S Argetsinger

¹Department of Molecular and Integrative Physiology, University of Michigan Medical School, Ann Arbor, MI 48109-5622, USA.

Journal of Cell Science

|April 14, 2011

Summary

This summary is machine-generated.

The SH2B1β protein

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Area of Science:

Cell Biology
Molecular Biology
Protein Trafficking

Background:

Protein localization is crucial for cellular function.
The adapter protein SH2B1β is implicated in human obesity.
Understanding SH2B1β's cellular transport is key to its function.

Purpose of the Study:

To investigate the mechanisms regulating SH2B1β localization.
To identify the role of the nuclear localization sequence (NLS) in SH2B1β transport.
To explore the functional consequences of SH2B1β's cellular location.

Main Methods:

Analysis of SH2B1β protein localization using various cell biology techniques.
Investigating protein-protein interactions and domain requirements for localization.
Studying the effects of post-translational modifications, such as phosphorylation, on SH2B1β trafficking.

Main Results:

The polybasic nuclear localization sequence (NLS) of SH2B1β targets it to both the nucleus and the plasma membrane (PM).
SH2B1β binds to the PM via electrostatic interactions, enhanced by its dimerization domain.
Phosphorylation of serine residues near the NLS releases SH2B1β from the PM, promoting nuclear entry.
SH2B1β's PM release and/or nuclear entry are essential for nerve growth factor (NGF)-induced gene expression and neurite outgrowth.

Conclusions:

The NLS of SH2B1β exhibits a dual role in protein localization to the nucleus and PM.
SH2B1β's dynamic cycling between cellular compartments, regulated by phosphorylation, is vital for its physiological functions.
These findings elucidate novel mechanisms of protein trafficking and signaling in response to NGF.