CPT1C

Last update 08 May 2025

Basic Info

Synonyms

Carnitine O-palmitoyltransferase 1, brain isoform, Carnitine O-palmitoyltransferase I, brain isoform, carnitine palmitoyltransferase 1C

+ [8]

Introduction

Palmitoyl thioesterase specifically expressed in the endoplasmic reticulum of neurons. Modulates the trafficking of the glutamate receptor, AMPAR, to plasma membrane through depalmitoylation of GRIA1 (PubMed:30135643). Also regulates AMPR trafficking through the regulation of SACM1L phosphatidylinositol-3-phosphatase activity by interaction in a malonyl-CoA dependent manner (By similarity). Binds malonyl-CoA and couples malonyl-CoA to ceramide levels, necessary for proper spine maturation and contributing to systemic energy homeostasis and appetite control (PubMed:16651524). Binds to palmitoyl-CoA, but does not have carnitine palmitoyltransferase 1 catalytic activity or at very low levels (PubMed:25751282, PubMed:30135643).

100 Clinical Results associated with CPT1C

100 Translational Medicine associated with CPT1C

0 Patents (Medical) associated with CPT1C

146

Literatures (Medical) associated with CPT1C

01 May 2025·Pharmacological Reviews

International Union of Basic and Clinical Pharmacology. CXIX. Fundamental insights and clinical relevance regarding the carnitine palmitoyltransferase family of enzymes

Review

Author: Fadó, Rut ; Rodríguez-Rodríguez, Rosalía ; Paraiso, West Kristian ; Baena, Miguel ; Zagmutt, Sebastián ; Reguera, Ana Cristina ; Casals, Núria

The carnitine palmitoyltransferases (CPTs) play a key role in controlling the oxidation of long-chain fatty acids and are potential therapeutic targets for diseases with a strong metabolic component, such as obesity, diabetes, and cancer. Four distinct proteins are CPT1A, CPT1B, CPT1C, and CPT2, differing in tissue expression and catalytic activity. CPT1s are finely regulated by malonyl-CoA, a metabolite whose intracellular levels reflect the cell's nutritional state. Although CPT1C does not exhibit significant catalytic activity, it is capable of modulating the functioning of other neuronal proteins. Structurally, all CPTs share a Y-shaped catalytic tunnel that allows the entry of 2 substrates and accommodation of the acyl group in a hydrophobic pocket. Several molecules targeting these enzymes have been described, some showing potential in normalizing blood glucose levels in diabetic patients, and others that, through a central mechanism, are anorexigenic and enhance energy expenditure. However, given the critical roles that CPTs play in certain tissues, such as the heart, liver, and brain, it is essential to fully understand the differences between the various isoforms. We analyze in detail the structure of these proteins, their cellular and physiological functions, and their potential as therapeutic targets in diseases such as obesity, diabetes, and cancer. We also describe drugs identified to date as having inhibitory or activating capabilities for these proteins. This knowledge will support the design of new drugs specific to each isoform, and the development of nanomedicines that can selectively target particular tissues or cells. SIGNIFICANCE STATEMENT: Carnitine palmitoyltransferase (CPT) proteins, as gatekeepers of fatty acid oxidation, have great potential as pharmacological targets to treat metabolic diseases like obesity, diabetes, and cancer. In recent years, significant progress has been made in understanding the 3-dimensional structure of CPTs and their pathophysiological functions. A deeper understanding of the differences between the various CPT family members will enable the design of selective drugs and therapeutic approaches with fewer side effects.

01 Apr 2025·Molecular Metabolism

CPT1C DEFICIENCY IN SF1 NEURONS IMPAIRS EARLY METABOLIC ADAPTATION TO DIETARY FATS, LEADING TO OBESITY

Article

Author: Fosch, A ; Rodríguez-Rodríguez, R ; Reguera, A C ; Freire-Agulleiro, O ; Miralpeix, C ; Cota, D ; Zizzari, P ; García-Chica, J ; Serra, D ; Zagmutt, S ; Casals, N ; Pizarro, D S ; Herrero, L ; Rodríguez-García, M ; Batallé, G ; López, M

SF1 neurons of the ventromedial hypothalamus (VMH) play a pivotal role in regulating body weight and adiposity, particularly in response to a high-fat diet (HFD), as well as in the recovery from insulin-induced hypoglycemia. While the brain-specific CPT1C isoform is well known for its role in controlling food intake and energy homeostasis, its function within specific hypothalamic neuronal populations remains largely unexplored. Here, we demonstrate that CPT1C in SF1 neurons is essential for appropriate responses to dietary fats. Mice deficient in CPT1C within SF1 neurons fail to adjust their caloric intake during initial HFD exposure, which is associated with impaired activation of the melanocortin system. Furthermore, these mice exhibit disrupted metabolic gene expression in the liver, muscle, and adipose tissue, leading to increased adiposity independently of food intake. In contrast, their response to glucose or insulin challenges remains intact. After long-term HFD exposure, SF1-Cpt1c-KO mice are more prone to developing obesity and glucose intolerance than control littermates, with males exhibiting a more severe phenotype. Interestingly, CPT1C deficiency in SF1 neurons also results in elevated hypothalamic endocannabinoid (eCB) levels under both chow and HFD conditions. We propose that this sustained eCB elevation reduces VMH activation by fatty acids and impairs the SF1-POMC drive upon fat intake. Our findings establish CPT1C in SF1 neurons as a critical regulator of VMH-driven dietary fat sensing, satiety, and lipid metabolic adaptation.

01 Mar 2025·Annals of Clinical and Translational Neurology

Expanding molecular and clinical spectrum of CPT1C‐associated hereditary spastic paraplegia (SPG73)—a case series

Article

Author: Alecu, Julian E. ; Schierbaum, Luca ; Brooks, Alexandra K. ; Tam, Amy ; Ebrahimi‐Fakhari, Darius ; Quiroz, Vicente

AbstractAutosomal‐dominant variants in the CPT1C gene have been associated with hereditary spastic paraplegia type 73 (SPG73), which typically presents with slowly progressive lower limb weakness and spasticity and is therefore considered a pure form of hereditary spastic paraplegia. However, we report two unrelated males with novel CPT1C variants (NM_001199753.2: patient 1: c.2057_2061del (p.Ile686SerfsTer8) and patient 2: c.2020‐1G>C (p.?)) who presented with lower limb spasticity at 4 and 3 years old, respectively. Both patients also experienced significant cognitive impairment, seizures, or neurobehavioral symptoms. These cases illustrate a broader and more complex clinical spectrum of SPG73, extending beyond the traditionally recognized pure motor symptoms.

Analysis

Perform a panoramic analysis of this field.

view full example data

AI Agents Built for Biopharma Breakthroughs

Accelerate discovery. Empower decisions. Transform outcomes.

Get started for free today!

Accelerate Strategic R&D decision making with Synapse, PatSnap’s AI-powered Connected Innovation Intelligence Platform Built for Life Sciences Professionals.

Start your data trial now!

Synapse data is also accessible to external entities via APIs or data packages. Empower better decisions with the latest in pharmaceutical intelligence.

Bio

Bio Sequences Search & Analysis

Chemical

Chemical Structures Search & Analysis

CPT1C

Basic Info

Related

Analysis