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Related Concept Videos

Phosphorylation01:02

Phosphorylation

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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...
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Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

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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...
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Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
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Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
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Gene Families01:57

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Gene families consist of groups of genes proposed to have originated from a common ancestor. Typically these arise through events in which a gene or genes are mistakenly duplicated during cell division. Unlike their parent genes (which are subject to selection pressure to maintain function), these gene copies do not need to preserve their sequences and may evolve at a relatively faster rate.
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Intrinsically Disordered Proteins02:18

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Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
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Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
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Disorder with consequence: Phosphorylation sites in HSPB5 yield distinct structural outcomes.

Natalie L Stone1, Maria K Janowska1, Lucas Narisawa2

  • 1Department of Biochemistry, University of Washington, Seattle, WA United States.

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|November 24, 2025
PubMed
Summary

Small heat shock protein B5 (HSPB5) phosphorylation regulates its structure and function. Different phosphorylation patterns on HSPB5 lead to distinct cellular outcomes and chaperone activities, impacting cellular stress responses.

Keywords:
HSPB5alphaB crystallinchaperoneintrinsic disorderphosphorylationsmall heat shock proteins

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Stress Response

Background:

  • Small heat shock proteins (sHSPs) like HSPB5 are crucial for cellular stress response.
  • Phosphorylation is a key mechanism regulating sHSP activity.
  • HSPB5 has three phosphorylation sites in its N-terminal region (NTR) that influence its function.

Purpose of the Study:

  • To investigate the impact of single and triple phospho-mimicry on HSPB5 oligomeric properties.
  • To understand how different phosphorylation events on HSPB5 lead to distinct cellular outcomes.
  • To elucidate the structural basis for altered chaperone activity in phosphorylated HSPB5.

Main Methods:

  • Utilized phospho-mimicking mutations at serine residues (S19, S45, S59) in HSPB5.
  • Assessed changes in oligomer size, subunit exchange, and hydrogen-deuterium protection patterns.
  • Evaluated the effect of phosphorylation on HSPB5's ability to delay the aggregation of γD-crystallin.

Main Results:

  • Single phosphorylation sites induced subtle changes in HSPB5 oligomerization and chaperone activity.
  • Triple phospho-mimicry resulted in significant structural and functional alterations of HSPB5.
  • The S45D phosphomimic demonstrated enhanced chaperone activity, with a structural rationale provided.

Conclusions:

  • Distinct phosphorylation events on HSPB5 lead to differential structural and functional outcomes.
  • Phosphorylation state critically modulates HSPB5's role as a cellular stress responder and chaperone.
  • Findings provide structural insights into the mechanism of HSPB5 regulation by phosphorylation.