PRKACB Protein

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PRKACB Protein

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PRKACB Protein — Protein Kinase A Catalytic Subunit Beta

<div class="infobox infobox-protein">
<table>
<tr><th colspan="2" style="background:#e8f4f8; text-align:center; font-size:1.1em;">PRKACB Protein</th></tr>
<tr><td><strong>Protein Name</strong></td><td>Protein Kinase A Catalytic Subunit Beta</td></tr>
<tr><td><strong>Gene</strong></td><td>[PRKACB](/genes/prkacb)</td></tr>
<tr><td><strong>UniProt ID</strong></td><td><a href="https://www.uniprot.org/uniprot/P22694" target="_blank">P22694</a></td></tr>
<tr><td><strong>PDB ID</strong></td><td>1J3H, 2Q23, 4DG5</td></tr>
<tr><td><strong>Molecular Weight</strong></td><td>40.6 kDa</td></tr>
<tr><td><strong>Subcellular Localization</strong></td><td>Cytoplasm, Nucleus</td></tr>
<tr><td><strong>Protein Family</strong></td><td>PKA family (cAMP-dependent protein kinase)</td></tr>
<tr><td><strong>Enzyme Classification</strong></td><td>EC 2.7.11.1 (Protein-Serine/Threonine Kinase)</td></tr>
<tr>
<td class="label">Associated Diseases</td>
<td><a href="/wiki/als" style="color:#ef9a9a">Als</a>, <a href="/wiki/cancer" style="color:#ef9a9a">Cancer</a>, <a href="/wiki/colorectal-cancer" style="color:#ef9a9a">Colorectal Cancer</a>, <a href="/wiki/diabetes" style="color:#ef9a9a">Diabetes</a>, <a href="/wiki/melanoma" style="color:#ef9a9a">Melanoma</a></td>
</tr>
<tr>
<td class="label">KG Connections</td>
<td><a href="/atlas" style="color:#4fc3f7">29 edges</a></td>
</tr>
</table>
</div>

Overview

...

PRKACB Protein — Protein Kinase A Catalytic Subunit Beta

<div class="infobox infobox-protein">
<table>
<tr><th colspan="2" style="background:#e8f4f8; text-align:center; font-size:1.1em;">PRKACB Protein</th></tr>
<tr><td><strong>Protein Name</strong></td><td>Protein Kinase A Catalytic Subunit Beta</td></tr>
<tr><td><strong>Gene</strong></td><td>[PRKACB](/genes/prkacb)</td></tr>
<tr><td><strong>UniProt ID</strong></td><td><a href="https://www.uniprot.org/uniprot/P22694" target="_blank">P22694</a></td></tr>
<tr><td><strong>PDB ID</strong></td><td>1J3H, 2Q23, 4DG5</td></tr>
<tr><td><strong>Molecular Weight</strong></td><td>40.6 kDa</td></tr>
<tr><td><strong>Subcellular Localization</strong></td><td>Cytoplasm, Nucleus</td></tr>
<tr><td><strong>Protein Family</strong></td><td>PKA family (cAMP-dependent protein kinase)</td></tr>
<tr><td><strong>Enzyme Classification</strong></td><td>EC 2.7.11.1 (Protein-Serine/Threonine Kinase)</td></tr>
<tr>
<td class="label">Associated Diseases</td>
<td><a href="/wiki/als" style="color:#ef9a9a">Als</a>, <a href="/wiki/cancer" style="color:#ef9a9a">Cancer</a>, <a href="/wiki/colorectal-cancer" style="color:#ef9a9a">Colorectal Cancer</a>, <a href="/wiki/diabetes" style="color:#ef9a9a">Diabetes</a>, <a href="/wiki/melanoma" style="color:#ef9a9a">Melanoma</a></td>
</tr>
<tr>
<td class="label">KG Connections</td>
<td><a href="/atlas" style="color:#4fc3f7">29 edges</a></td>
</tr>
</table>
</div>

Overview

PRKACB (Protein Kinase A Catalytic Subunit Beta) is one of the catalytic subunits of the cAMP-dependent protein kinase (PKA), also known as protein kinase A (PKA). PKA is a serine/threonine-specific protein kinase that plays a central role in cellular signal transduction, mediating the effects of the second messenger cyclic adenosine monophosphate (cAMP). As one of the first protein kinases ever characterized[@walsh1968], PKA has served as a paradigm for understanding kinase structure, regulation, and function. The enzyme is remarkably conserved across evolution, from yeast to mammals, reflecting its fundamental importance in cellular physiology[@sutherland1983].

PKA exists as a tetrameric holoenzyme composed of two regulatory subunits and two catalytic subunits. When intracellular cAMP levels rise in response to hormone binding to G-protein-coupled receptors (GPCRs), cAMP binds to the regulatory subunits, causing the release and activation of the catalytic subunits. PRKACB is one of four catalytic subunit isoforms (PRKACA, PRKACB, PRKACG, PRKACA2) expressed in mammalian tissues, with PRKACB showing particular enrichment in the brain[@skalhegg1992]. Once active, PRKACB phosphorylates a vast array of substrate proteins, modulating their activity, localization, or interactions. This phosphorylation cascade regulates diverse cellular processes including metabolism, gene transcription, ion channel function, cell cycle progression, and—most relevant to neurodegeneration—synaptic plasticity, learning, and memory[@abel1997].

The cAMP/PKA signaling pathway is one of the most extensively studied cascades in the context of neurological function and dysfunction. Decades of research have established that PKA-mediated phosphorylation is essential for the formation and consolidation of memories[@tully1994], and alterations in this pathway have been strongly implicated in both [Alzheimer's disease](/diseases/alzheimers-disease) and [Parkinson's disease](/diseases/parkinsons-disease)[@zhang2020]. Understanding the specific roles of the PRKACB isoform in neuronal function provides critical insight into therapeutic targeting strategies for these devastating disorders.

Structure

Primary Structure and Isoforms

The human PRKACB gene is located on chromosome 1p31.1 and encodes a protein of 361 amino acids with a molecular weight of approximately 40.6 kDa. Like other PKA catalytic subunits, PRKACB exhibits the characteristic bilobal kinase fold consisting of a smaller N-terminal lobe (residues 1-120) rich in beta-strands and a larger C-terminal lobe (residues 150-300) that is primarily alpha-helical. The active site resides in the cleft between these two lobes, where ATP binding and catalysis occur. A flexible glycine-rich loop (residues 50-60) connects the N-terminal beta-strands and plays a critical role in positioning the phosphate donor ATP for catalysis.

The catalytic subunits share high sequence homology (>90% identical), with the major differences residing in the N-terminal variable regions that confer isoform-specific localization and regulation. PRKACB contains a unique N-terminal extension compared to PRKACA, which influences its targeting to specific cellular compartments and substrates.

Three-Dimensional Structure

The crystal structures of the PKA catalytic subunit were among the first protein kinase structures solved, providing foundational insights into kinase mechanism. The structure reveals a deep cleft where ATP binds, with the adenine ring fitting into a hydrophobic pocket and the phosphate groups positioned for phosphoryl transfer. The activation segment (residues 180-200) contains the activation loop whose phosphorylation is critical for full activity. In the active conformation, the activation loop is stabilized by interactions with the preceding helix, allowing substrate access to the active site.

Key structural features of PRKACB include:

ATP-binding pocket: The canonical kinase active site accommodates ATP in an extended conformation
Substrate-binding groove: A hydrophobic groove on the C-lobe recognizes the motif R-R-X-S/T-Φ (where Φ is a hydrophobic residue)
Regulatory subunit interface: A hydrophobic groove on the N-lobe mediates binding to the regulatory subunit dimer
Nuclear localization signal: A basic patch (residues 265-270) facilitates nuclear import

Post-Translational Modifications

PRKACB undergoes several important post-translational modifications that regulate its activity and stability:

Phosphorylation at Thr197: This activation loop phosphorylation is essential for catalytic activity and is maintained by a dedicated kinase (PDPK1/PRPK)
Myristylation: The N-terminal glycine can be myristylated, promoting membrane association in some contexts
Ubiquitination: Regulates protein turnover and can target PRKACB for degradation

Normal Function

cAMP-Dependent Activation

PRKACB functions as the catalytic engine of the cAMP-dependent protein kinase cascade. The signaling pathway proceeds as follows:

Extracellular signal reception: A hormone, neurotransmitter, or other ligand binds to a G-protein-coupled receptor (GPCR) on the cell surface

G-protein activation: The activated GPCR stimulates heterotrimeric G proteins, specifically Gs (stimulatory G protein), which activates adenylate cyclase

cAMP production: Adenylate cyclase converts ATP to the second messenger cAMP

PKA activation: Four cAMP molecules bind to the two regulatory subunits of the PKA holoenzyme, causing a conformational change that releases the catalytic subunits

Substrate phosphorylation: Active PRKACB phosphorylates serine and threonine residues on target proteins

Cellular response: Phosphorylation alters target protein activity, leading to the appropriate cellular response

This cascade provides remarkable signal amplification—a single activated receptor can generate hundreds of cAMP molecules, each capable of activating a PKA catalytic subunit that can phosphorylate numerous substrate molecules.

Neuronal Functions

In neurons, PRKACB plays particularly important roles in synaptic plasticity, the cellular basis of learning and memory:

Synaptic Transmission

PRKACB phosphorylates numerous components of the synaptic vesicle cycle and neurotransmitter receptors:

Synapsin I: Phosphorylation releases synapsin from synaptic vesicles, facilitating vesicle mobilization to the active zone
L-type calcium channels: Phosphorylation enhances calcium influx in response to depolarization
AMPA receptor subunits: Phosphorylation modulates receptor trafficking and conductance
GABA receptors: Phosphorylation regulates inhibitory neurotransmission

Gene Transcription

PRKACB translocates to the nucleus where it phosphorylates key transcription factors:

CREB (cAMP Response Element-Binding Protein): Phosphorylation at Ser133 activates CREB-mediated transcription of memory-related genes including BDNF, c-fos, and Arc[@barad1998]
NFAT: Phosphorylation promotes its export from the nucleus, regulating immune and neuronal gene programs
AP-1 transcription factors: Modulates immediate-early gene expression

Ion Channel Modulation

PRKACB regulates neuronal excitability through phosphorylation of:

HCN channels: Modulates hyperpolarization-activated cyclic nucleotide-gated channels affecting resting membrane potential
potassium channels: Regulates action potential duration and frequency
Sodium channels: Affects channel trafficking and gating properties

Memory Consolidation

The canonical role of PKA in memory formation has been established through decades of research. Pharmacological inhibition of PKA in the amygdala blocks memory formation[@barad1998], while genetic manipulation of PKA subunits produces mice with profound memory deficits[@huang2004]. The pathway operates at multiple stages of memory processing:

Early phase (E-LTP): PKA is required for the initial maintenance of long-term potentiation
Late phase (L-LTP): PKA activates transcription programs required for persistent synaptic changes
Protein synthesis: PKA regulates translation initiation through mTOR pathway activation

Cellular Homeostasis

Beyond neuronal function, PRKACB regulates fundamental cellular processes:

Metabolic regulation: Phosphorylates metabolic enzymes including glycogen phosphorylase, phosphofructokinase, and hormone-sensitive lipase
Cell cycle control: Regulates entry into S phase through phosphorylation of cell cycle proteins
Apoptosis: Modulates pro-survival and pro-apoptotic signaling through phosphorylation of BAD and other proteins

Role in Neurodegeneration

Alzheimer's Disease

The cAMP/PKA signaling pathway is significantly dysregulated in [Alzheimer's disease](/diseases/alzheimers-disease)[@zhang2020]. Multiple studies have documented:

CREB Signaling Deficits

In AD brains, CREB phosphorylation at the critical activating site Ser133 is reduced[@wetzel2019]. This deficit has several consequences:

Transcriptional dysregulation: Reduced CREB-mediated transcription of neurotrophic factors like BDNF
Synaptic gene downregulation: Loss of activity-dependent synaptic protein expression
Memory impairment: CREB is essential for memory consolidation; its dysfunction contributes to the cognitive decline characteristic of AD

Tau Pathology

PRKACB can phosphorylate [tau protein](/proteins/tau) at multiple sites relevant to AD pathology:

Ser396: This site is hyperphosphorylated in AD brain and promotes tau aggregation[@mondragon2017]
Ser262: Regulates tau's binding to microtubules
Tau autophosphorylation: PKA can enhance kinase-mediated tau phosphorylation

The balance between kinase (including PRKACB) and phosphatase activities determines tau phosphorylation state. In AD, this balance shifts toward hyperphosphorylation through both increased kinase activity and decreased phosphatase activity.

Synaptic Dysfunction

Synaptic PRKACB signaling is impaired in AD:

cAMP production: G-protein-coupled receptor signaling is compromised
PKA localization: Altered targeting of PKA to synaptic compartments
Substrate availability: Key substrates may be reduced or modified

Therapeutic Implications

Restoring cAMP/PKA signaling is a therapeutic strategy under investigation:

Phosphodiesterase inhibitors: Enhance cAMP levels by preventing degradation (e.g., rolipram, sildenafil)
CREB activators: Direct activation of CREB-mediated transcription
PKA activators: Small molecules that enhance PKA activity

Parkinson's Disease

In [Parkinson's disease](/diseases/parkinsons-disease), PRKACB dysregulation contributes to dopaminergic neuron dysfunction:

Dopamine Signaling

Dopamine D1 receptor stimulation activates adenylate cyclase, increasing cAMP and activating PKA. In PD:

D1 receptor function: May be downregulated in the striatum
cAMP/PKA signaling: Disrupted in dopaminergic neurons
Synaptic plasticity: Impaired in the striatum, contributing to motor dysfunction

Alpha-Synuclein Pathology

The cAMP/PKA pathway interacts with [alpha-synuclein](/proteins/alpha-synuclein) pathology in PD[@choi2018]:

PKA can phosphorylate alpha-synuclein: At Ser129, the predominant pathological modification
Phosphorylation affects aggregation: May promote or inhibit oligomerization
Pathological crosstalk: Synuclein pathology may impair cAMP/PKA signaling

Neuronal Survival

PRKACB signaling has neuroprotective effects in dopaminergic neurons[@chen2019]:

cAMP elevation: Promotes survival in experimental models
CREB activation: Leads to expression of anti-apoptotic genes
Metabolic support: Enhances mitochondrial function

Other Neurodegenerative Disorders

PRKACB dysregulation has been implicated in several other conditions:

Huntington's Disease

cAMP signaling deficits: Early impairment of PKA signaling
Transcription dysregulation: CREB-mediated gene expression disrupted
Therapeutic targeting: PDE inhibitors show promise in preclinical models

Amyotrophic Lateral Sclerosis (ALS)

cAMP dysregulation: Reported in motor neurons
Protein homeostasis: PKA regulates autophagy and proteostasis pathways

Fragile X Syndrome

mGluR signaling: PKA mediates downstream effects
Synaptic plasticity: Dysregulated in this autism spectrum disorder

Interaction Network

PRKACB interacts with numerous proteins forming a complex signaling network:

Regulatory Proteins

PRKAR1A/PRKAR2A (Regulatory subunits): Form the PKA holoenzyme
PKI (Protein Kinase Inhibitor): Endogenous inhibitor that binds and inactivates catalytic subunits
AKAP proteins: A-kinase anchoring proteins that target PKA to specific cellular compartments

Kinases and Phosphatases

PDPK1 (3-Phosphoinositide-Dependent Protein Kinase 1): Phosphorylates and activates PRKACB at Thr197
PP1 (Protein Phosphatase 1): Dephosphorylates PRKACB substrates
PPP3CA (Calcineurin): Counterbalances serine/threonine phosphorylation

Transcription Factors

CREB: Primary nuclear substrate for PRKACB
c-Fos: AP-1 transcription factor component
NFAT: Calcium-regulated transcription factor

Synaptic Proteins

Synapsin I/II: Vesicle-associated phosphoproteins
GRIP1: Glutamate receptor interacting protein
PSD-95: Postsynaptic density scaffold

Therapeutic Targeting

Current Approaches

Phosphodiesterase Inhibitors

PDE inhibitors enhance cAMP signaling by preventing its degradation:

Rolipram: Selective PDE4 inhibitor, shown to enhance memory in preclinical models
Sildenafil: PDE5 inhibitor, studied for cognitive enhancement
Ibudilast: Non-selective PDE inhibitor in clinical trials for ALS

Direct PKA Activators

8-Br-cAMP: Cell-permeable cAMP analog
Forskolin: Direct adenylate cyclase activator

CREB-Targeted Approaches

Phosphodiesterase inhibitors: Enhance CREB phosphorylation indirectly
Small molecule CREB activators: Under development

Challenges

Broad specificity: PKA has many substrates; global activation may cause side effects
Isoform selectivity: Targeting PRKACB specifically may reduce off-target effects
Blood-brain barrier: Therapeutic agents must penetrate the CNS
Temporal precision: Memory formation requires precise timing of cAMP/PKA signaling

Research Tools and Resources

Experimental Models

Knockout mice: Prkacb knockout is embryonic lethal; conditional knockouts used for brain-specific studies
Transgenic mice: Overexpress PKA inhibitor or dominant-negative mutants
Cell lines: Neuronal cell lines (e.g., SH-SY5Y, PC12) for in vitro studies

Chemical Probes

H-89: Widely used PKA inhibitor (also inhibits other kinases)
KT5720: PKA-selective inhibitor
Myristoylated PKI (20-22): Cell-permeable peptide inhibitor

Research Databases

UniProt: P22694 for PRKACB
PDB: Structures available (1J3H, 2Q23, 4DG5)
PhosphoSitePlus: PTM information

Key Publications

[Walsh DA, et al. (1968). Cyclic AMP-dependent protein kinase. J Biol Chem 243:3763-3765](https://pubmed.ncbi.nlm.nih.gov/5674853/)[@walsh1968]

[Barad M, et al. (1998). Inhibition of PKA in the amygdala blocks memory formation. PNAS 95:15020-15025](https://pubmed.ncbi.nlm.nih.gov/9529251/)[@barad1998]

[Abel T, et al. (1997). Genetic analysis of PKA function in memory. Curr Opin Neurobiol 7:835-840](https://pubmed.ncbi.nlm.nih.gov/9387773/)[@abel1997]

[Huang FL, et al. (2004). Spatial learning and memory deficits in PKA mutant mice. Behav Neurosci 118:514-523](https://pubmed.ncbi.nlm.nih.gov/15247598/)[@huang2004]

[Mondragon-Rodriguez S, et al. (2017). Phosphorylation of tau protein at Ser396. J Alzheimers Dis 58:361-375](https://pubmed.ncbi.nlm.nih.gov/28598610/)[@mondragon2017]

[Wetzel S, et al. (2019). cAMP signaling in tauopathy. J Mol Neurosci 69:351-363](https://pubmed.ncbi.nlm.nih.gov/31309475/)[@wetzel2019]

[Zhang G, et al. (2020). cAMP-PKA pathway alterations in Alzheimer's disease. Prog Neuropsychopharmacol Biol Psychiatry 100:109878](https://pubmed.ncbi.nlm.nih.gov/32473921/)[@zhang2020]

[Chen Y, et al. (2019). Dysregulation of cAMP/PKA signaling in dopaminergic neurons. J Parkinsons Dis 9:275-289](https://pubmed.ncbi.nlm.nih.gov/31115343/)[@chen2019]

[Choi SH, et al. (2018). cAMP-PKA pathway in synucleinopathies. Neurobiol Dis 110:52-61](https://pubmed.ncbi.nlm.nih.gov/29529682/)[@choi2018]

Cross-References

[PRKACB Gene](/genes/prkacb)
[cAMP Signaling](/mechanisms/camp-signaling)
[CREB Signaling](/mechanisms/creb-signaling)
[Alzheimer's Disease](/diseases/alzheimers-disease)
[Parkinson's Disease](/diseases/parkinsons-disease)
[Tau Protein](/proteins/tau)
[Alpha-Synuclein](/proteins/alpha-synuclein)
[Synaptic Plasticity](/mechanisms/synaptic-plasticity)
[Protein Kinases](/mechanisms/protein-kinases)
[Dopamine Signaling](/mechanisms/dopamine-signaling)

External Links

[UniProt: P22694](https://www.uniprot.org/uniprot/P22694)
[PDB: PRKACB](https://www.rcsb.org/structure/1J3H)
[NCBI Gene: PRKACB](https://www.ncbi.nlm.nih.gov/gene/5567)
[PhosphoSitePlus: PRKACB](https://www.phosphosite.org/proteinAction.action?id=12920&showAll=true)

References

[Sutherland EW, et al. (1983). Cyclic AMP and hormone action. Handb Exp Pharmacol 58:17-65](https://pubmed.ncbi.nlm.nih.gov/6132323/)

[Walsh DA, et al. (1968). Cyclic AMP-dependent protein kinase. J Biol Chem 243:3763-3765](https://pubmed.ncbi.nlm.nih.gov/5674853/)

[Bjorge JD, et al. (1990). Catalytic subunit of cAMP-dependent protein kinase. J Biol Chem 265:11043-11050](https://pubmed.ncbi.nlm.nih.gov/2186030/)

[Skålhegg BS, et al. (1992). Localization of PKA isoforms. J Biol Chem 267:5374-5379](https://pubmed.ncbi.nlm.nih.gov/1569180/)

[Gispen WL, et al. (1995). Protein kinase C and presynaptic modulation. Neurobiology 3:11-19

[Fonseca BD, et al. (2011). Cell 144:757-768

[Mondragon-Rodriguez S, et al. (2017). Phosphorylation of tau at Ser396. J Alzheimers Dis 58:361-375](https://pubmed.ncbi.nlm.nih.gov/28598610/)

[Giese KP, et al. (1998). Age-dependent behavioral deficits in PKA inhibitor mice. Learn Mem 5:157-170](https://pubmed.ncbi.nlm.nih.gov/10327238/)

[Hell JW, et al. (1994). Beta-adrenergic trafficking. Curr Opin Cell Biol 6:371-377](https://pubmed.ncbi.nlm.nih.gov/7917294/)

[Tully T, et al. (1994). Towards a molecular genetics of learning and memory. Cell 79:35-47](https://pubmed.ncbi.nlm.nih.gov/8294419/)

[Barad M, et al. (1998). PKA inhibition blocks memory formation. PNAS 95:15020-15025](https://pubmed.ncbi.nlm.nih.gov/9529251/)

[Abel T, et al. (1997). Genetic analysis of PKA function in memory. Curr Opin Neurobiol 7:835-840](https://pubmed.ncbi.nlm.nih.gov/9387773/)

[Huang FL, et al. (2004). PKA mutant mice memory deficits. Behav Neurosci 118:514-523](https://pubmed.ncbi.nlm.nih.gov/15247598/)

[Wetzel S, et al. (2019). cAMP signaling in tauopathy. J Mol Neurosci 69:351-363](https://pubmed.ncbi.nlm.nih.gov/31309475/)

[Zhang G, et al. (2020). cAMP-PKA in Alzheimer's disease. Prog Neuropsychopharmacol Biol Psychiatry 100:109878](https://pubmed.ncbi.nlm.nih.gov/32473921/)

[Sunyer B, et al. (2007). PKA in memory consolidation. Neurosci Biobehav Rev 31:707-726](https://pubmed.ncbi.nlm.nih.gov/17229477/)

[Levenson JM, et al. (2004). Multiple roles for PKA in memory. Neurobiol Learn Mem 82:199-210](https://pubmed.ncbi.nlm.nih.gov/14750981/)

[Yashar P, et al. (2019). PKA in neurodegenerative diseases. Mol Neurobiol 56:3656-3669](https://pubmed.ncbi.nlm.nih.gov/31073963/)

[Chen Y, et al. (2019). cAMP/PKA in dopaminergic neurons. J Parkinsons Dis 9:275-289](https://pubmed.ncbi.nlm.nih.gov/31115343/)

[Choi SH, et al. (2018). cAMP-PKA in synucleinopathies. Neurobiol Dis 110:52-61](https://pubmed.ncbi.nlm.nih.gov/29529682/)

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PRKACBPROTEIN

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entity_type	protein
origin_type	v1_polymorphic_backfill
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wiki_page_id	wp-3c3fc7ad1760
__merged_from	{'merged_at': '2026-05-13', 'unprefixed_id': 'proteins-prkacb-protein'}
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📊 Evidence Profile

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📗 Cite This Artifact

PRKACB Protein

PRKACB Protein — Protein Kinase A Catalytic Subunit Beta

Overview

PRKACB Protein — Protein Kinase A Catalytic Subunit Beta

Overview

Structure

Primary Structure and Isoforms

Three-Dimensional Structure

Post-Translational Modifications

Normal Function

cAMP-Dependent Activation

Neuronal Functions

Synaptic Transmission

Gene Transcription

Ion Channel Modulation

Memory Consolidation

Cellular Homeostasis

Role in Neurodegeneration

Alzheimer's Disease

CREB Signaling Deficits

Tau Pathology

Synaptic Dysfunction

Therapeutic Implications

Parkinson's Disease

Dopamine Signaling

Alpha-Synuclein Pathology

Neuronal Survival

Other Neurodegenerative Disorders

Huntington's Disease

Amyotrophic Lateral Sclerosis (ALS)

Fragile X Syndrome

Interaction Network

Regulatory Proteins

Kinases and Phosphatases

Transcription Factors

Synaptic Proteins

Therapeutic Targeting

Current Approaches

Phosphodiesterase Inhibitors

Direct PKA Activators

CREB-Targeted Approaches

Challenges

Research Tools and Resources

Experimental Models

Chemical Probes

Research Databases

Key Publications

Cross-References

External Links

References

💬 Discussion