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Article ; Online: CD36 ectodomain phosphorylation blocks thrombospondin-1 binding: structure-function relationships and regulation by protein kinase C.

Chu, Ling-Yun / Silverstein, Roy L

Arteriosclerosis, thrombosis, and vascular biology

2012 Volume 32, Issue 3, Page(s) 760–767

Abstract: ... binding in vitro and explored mechanisms regulating phosphorylation by protein kinase C (PKC) in melanoma ... induce detectable extracellular or cell surface-associated kinase activity, and both cycloheximide and ... phosphorylation and decreased ligand-mediated recruitment of Src-family proteins to CD36. PMA treatment did not ...

Abstract	Objective: CD36 phosphorylation on its extracellular domain inhibits binding of thrombospondin-1. The mechanisms of cellular CD36 ectodomain phosphorylation and whether it can be regulated in cells are not known. We determined structure-function relationships of CD36 phosphorylation related to thrombospondin-1 peptide binding in vitro and explored mechanisms regulating phosphorylation by protein kinase C (PKC) in melanoma cells. Methods and results: Phosphorylation of CD36 peptide on Thr92 by PKCα suppressed binding of thrombospondin-1 peptides in vitro, and the level of inhibition correlated with the level of phosphorylation. Basal phosphorylation levels of CD36 in vivo in platelets, endothelial cells, and melanoma cells were assessed by immunoprecipitation and immunoblot and were found to be very low. Treatment of CD36-transfected melanoma cells with phorbol 12-myristate 13-acetate (PMA), a PKC activator, induced substantial CD36 phosphorylation and decreased ligand-mediated recruitment of Src-family proteins to CD36. PMA treatment did not induce detectable extracellular or cell surface-associated kinase activity, and both cycloheximide and brefeldin A blocked CD36 phosphorylation. Conclusion: New protein synthesis and trafficking through the Golgi are required for PMA-induced CD36 phosphorylation, suggesting that phosphorylation probably occurs intracellularly. These studies suggest a novel in vivo pathway for CD36 phosphorylation that modulates cellular affinity for thrombospondin-related proteins to blunt vascular cell signaling.
MeSH term(s)	Blotting, Western ; CD36 Antigens/chemistry ; CD36 Antigens/genetics ; CD36 Antigens/metabolism ; Cell Line, Tumor ; Endothelial Cells/enzymology ; Enzyme Activation ; Enzyme Activators/pharmacology ; Golgi Apparatus/metabolism ; Humans ; Immunoprecipitation ; Melanoma/enzymology ; Melanoma/genetics ; Phosphorylation ; Protein Binding ; Protein Conformation ; Protein Interaction Domains and Motifs ; Protein Interaction Mapping ; Protein Kinase C-alpha/metabolism ; Protein Synthesis Inhibitors/pharmacology ; Protein Transport ; Structure-Activity Relationship ; Tetradecanoylphorbol Acetate/pharmacology ; Thrombospondin 1/chemistry ; Thrombospondin 1/metabolism ; Time Factors ; Transfection ; src-Family Kinases/metabolism
Chemical Substances	CD36 Antigens ; Enzyme Activators ; Protein Synthesis Inhibitors ; Thrombospondin 1 ; src-Family Kinases (EC 2.7.10.2) ; PRKCA protein, human (EC 2.7.11.13) ; Protein Kinase C-alpha (EC 2.7.11.13) ; Tetradecanoylphorbol Acetate (NI40JAQ945)
Language	English
Publishing date	2012-01-12
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1221433-4
ISSN	1524-4636 ; 1079-5642
ISSN (online)	1524-4636
ISSN	1079-5642
DOI	10.1161/ATVBAHA.111.242511
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Zs.A 1705: Show issues

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Article ; Online: Structure-based discovery of small molecule inhibitors of FKBP51-Hsp90 protein-protein interaction.

Wang, Lisha / Kumar, Rajnish / Winblad, Bengt / Pavlov, Pavel F

European journal of medicinal chemistry

2024 Volume 270, Page(s) 116356

Abstract: ... of potent and selective inhibitors of FKBP51-Hsp90 protein-protein interaction using a structure-based ... towards regulation of FKBP51 function and more generally, Hsp90 function via its interaction with TPR co-chaperones. ... and activation of hundreds of important clients such as kinases, steroid hormone receptors ...

Abstract	The heat shock protein 90 kDa (Hsp90) molecular chaperone machinery is responsible for the folding and activation of hundreds of important clients such as kinases, steroid hormone receptors, transcription factors, etc. This process is dynamically regulated in an ATP-dependent manner by Hsp90 co-chaperones including a group of tetratricopeptide (TPR) motif proteins that bind to the C-terminus of Hsp90. Among these TPR containing co-chaperones, FK506-binding protein 51 kDa (FKBP51) is reported to play an important role in stress-related pathologies, psychiatric disorders, Alzheimer's disease, and cancer, making FKBP51-Hsp90 interaction a potential therapeutic target. In this study, we report identification of potent and selective inhibitors of FKBP51-Hsp90 protein-protein interaction using a structure-based virtual screening approach. Upon in vitro evaluation, the identified hits show a considerable degree of selectivity towards FKBP51 over other TPR proteins, particularly for highly homologous FKBP52. Tyr355 of FKBP51 emerged as an important contributor to inhibitor's specificity. Additionally, we demonstrate the impact of these inhibitors on cellular energy metabolism, and neurite outgrowth, which are subjects of FKBP51 regulation. Overall, the results from this study highlight a novel pharmacological approach towards regulation of FKBP51 function and more generally, Hsp90 function via its interaction with TPR co-chaperones.
MeSH term(s)	Humans ; Protein Binding ; Tacrolimus Binding Proteins/metabolism ; HSP90 Heat-Shock Proteins/metabolism ; Molecular Chaperones ; Transcription Factors/metabolism
Chemical Substances	Tacrolimus Binding Proteins (EC 5.2.1.-) ; HSP90 Heat-Shock Proteins ; Molecular Chaperones ; Transcription Factors
Language	English
Publishing date	2024-03-28
Publishing country	France
Document type	Journal Article
ZDB-ID	188597-2
ISSN	1768-3254 ; 0009-4374 ; 0223-5234
ISSN (online)	1768-3254
ISSN	0009-4374 ; 0223-5234
DOI	10.1016/j.ejmech.2024.116356
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Zs.B 784: Show issues

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Article ; Online: Computational analysis of regulatory regions in human protein kinases.

Pei, Jimin / Cong, Qian

Protein science : a publication of the Protein Society

2023 Volume 32, Issue 10, Page(s) e4764

Abstract: ... roles in different aspects of protein function. However, studying these interactions and ... intramolecular interactions between human protein kinase domains (KDs) and potential regulatory regions ... allosteric regulation of kinase activity. We also identified prevalent interactions between human KDs and their flanking ...

Abstract	Eukaryotic proteins often feature modular domain structures comprising globular domains that are connected by linker regions and intrinsically disordered regions that may contain important functional motifs. The intramolecular interactions of globular domains and nonglobular regions can play critical roles in different aspects of protein function. However, studying these interactions and their regulatory roles can be challenging due to the flexibility of nonglobular regions, the long insertions separating interacting modules, and the transient nature of some interactions. Obtaining the experimental structures of multiple domains and functional regions is more difficult than determining the structures of individual globular domains. High-quality structural models generated by AlphaFold offer a unique opportunity to study intramolecular interactions in eukaryotic proteins. In this study, we systematically explored intramolecular interactions between human protein kinase domains (KDs) and potential regulatory regions, including globular domains, N- and C-terminal tails, long insertions, and distal nonglobular regions. Our analysis identified intramolecular interactions between human KDs and 35 different types of globular domains, exhibiting a variety of interaction modes that could contribute to orthosteric or allosteric regulation of kinase activity. We also identified prevalent interactions between human KDs and their flanking regions (N- and C-terminal tails). These interactions exhibit group-specific characteristics and can vary within each specific kinase group. Although long-range interactions between KDs and nonglobular regions are relatively rare, structural details of these interactions offer new insights into the regulation mechanisms of several kinases, such as HASPIN, MAPK7, MAPK15, and SIK1B.
Language	English
Publishing date	2023-09-13
Publishing country	United States
Document type	Journal Article
ZDB-ID	1106283-6
ISSN	1469-896X ; 0961-8368
ISSN (online)	1469-896X
ISSN	0961-8368
DOI	10.1002/pro.4764
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Zs.A 3407: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Article: Protein kinase C: structure, function, and regulation.

Newton, A C

The Journal of biological chemistry

1995 Volume 270, Issue 48, Page(s) 28495–28498

MeSH term(s)	Phosphorylation ; Protein Conformation ; Protein Kinase C/chemistry ; Protein Kinase C/metabolism ; Substrate Specificity
Chemical Substances	Protein Kinase C (EC 2.7.11.13)
Language	English
Publishing date	1995-12-01
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, U.S. Gov't, P.H.S. ; Review
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.270.48.28495
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Article ; Online: Regulation of Sertoli cell function by planar cell polarity (PCP) protein Fjx1.

Bu, Tiao / Li, Xinyao / Wang, Lingling / Wu, Xiaolong / Gao, Sheng / Yun, Damin / Li, Linxi / Sun, Fei / Cheng, C Yan

Molecular and cellular endocrinology

2023 Volume 571, Page(s) 111936

Abstract: Four-jointed box kinase 1 (Fjx1) is a planar cell polarity (PCP) protein and a member of the Fat ... respectively, consistent with the role of Fjx1 as a Golgi-associated Ser/Thr kinase that modulates the Fat (and ... and regulatory proteins, its KD was found to down-regulate Fat1 (but not Fat2, 3, and 4) and to up ...

Abstract	Four-jointed box kinase 1 (Fjx1) is a planar cell polarity (PCP) protein and a member of the Fat (FAT atypical cadherin 1)/Dchs (Dachsous cadherin-related protein)/Fjx1 PCP complex. Fjx1 is also a non-receptor Ser/Thr protein kinase capable of phosphorylating Fat1 at is extracellular cadherin domains when it is being transported across the Golgi system. As such, Fjx1 is a Golgi-based regulator of Fat1 function by determining its extracellular deposition. Herein, Fjx1 was found to localize across the Sertoli cell cytoplasm, partially co-localized with the microtubules (MTs) across the seminiferous epithelium. It was most notable at the apical ES (ectoplasmic specialization) and basal ES, displaying distinctive stage-specific expression. The apical ES and basal ES are the corresponding testis-specific cell adhesion ultrastructures at the Sertoli-elongated spermatid interface and the Sertoli cell-cell interface, respectively, consistent with the role of Fjx1 as a Golgi-associated Ser/Thr kinase that modulates the Fat (and/or Dchs) integral membrane proteins. Its knockdown (KD) by RNAi using specific Fjx1 siRNA duplexes versus non-targeting negative control siRNA duplexes was found to perturb the Sertoli cell tight junction function, as well as perturbing the function and organization of MT and actin. While Fjx1 KD did not affect the steady-state levels of almost two dozens of BTB-associated Sertoli cell proteins, including structural and regulatory proteins, its KD was found to down-regulate Fat1 (but not Fat2, 3, and 4) and to up-regulate Dchs1 (but not Dchs2) expression. Based on results of biochemical analysis, Fjx1 KD was found to be capable of abolishing phosphorylation of its putative substrate Fat1 at its Ser/Thr sites, but not at its Tyr site, illustrating an intimate functional relationship of Fjx1 and Fat1 in Sertoli cells.
MeSH term(s)	Rats ; Animals ; Male ; Sertoli Cells/metabolism ; Spermatogenesis/genetics ; Cell Polarity ; Rats, Sprague-Dawley ; Testis/metabolism ; Seminiferous Epithelium/metabolism ; Cadherins/metabolism ; RNA, Small Interfering/metabolism ; Blood-Testis Barrier/metabolism
Chemical Substances	Cadherins ; RNA, Small Interfering
Language	English
Publishing date	2023-04-27
Publishing country	Ireland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	187438-x
ISSN	1872-8057 ; 0303-7207
ISSN (online)	1872-8057
ISSN	0303-7207
DOI	10.1016/j.mce.2023.111936
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Zs.A 1127: Show issues

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Article ; Online: The inhibitory mechanism of a small protein reveals its role in antimicrobial peptide sensing.

Jiang, Shan / Steup, Lydia C / Kippnich, Charlotte / Lazaridi, Symela / Malengo, Gabriele / Lemmin, Thomas / Yuan, Jing

Proceedings of the National Academy of Sciences of the United States of America

2023 Volume 120, Issue 41, Page(s) e2309607120

Abstract: ... small protein, MgrB, which represses the activity of the sensor kinase PhoQ and is widely distributed ... of cross-linking approaches with functional assays and protein dynamic simulations revealed structural ... PhoQ via derepression. Our findings reveal the inhibitory mechanism of the small protein MgrB and ...

Abstract	A large number of small membrane proteins have been uncovered in bacteria, but their mechanism of action has remained mostly elusive. Here, we investigate the mechanism of a physiologically important small protein, MgrB, which represses the activity of the sensor kinase PhoQ and is widely distributed among enterobacteria. The PhoQ/PhoP two-component system is a master regulator of the bacterial virulence program and interacts with MgrB to modulate bacterial virulence, fitness, and drug resistance. A combination of cross-linking approaches with functional assays and protein dynamic simulations revealed structural rearrangements due to interactions between MgrB and PhoQ near the membrane/periplasm interface and along the transmembrane helices. These interactions induce the movement of the PhoQ catalytic domain and the repression of its activity. Without MgrB, PhoQ appears to be much less sensitive to antimicrobial peptides, including the commonly used C18G. In the presence of MgrB, C18G promotes MgrB to dissociate from PhoQ, thus activating PhoQ via derepression. Our findings reveal the inhibitory mechanism of the small protein MgrB and uncover its importance in antimicrobial peptide sensing.
MeSH term(s)	Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Antimicrobial Peptides ; Membrane Proteins/metabolism ; Periplasm/metabolism ; Gene Expression Regulation, Bacterial
Chemical Substances	Bacterial Proteins ; Antimicrobial Peptides ; Membrane Proteins
Language	English
Publishing date	2023-10-04
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.2309607120
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Zs.A 1148: Show issues

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Article ; Online: The Roc domain of LRRK2 as a hub for protein-protein interactions: a focus on PAK6 and its impact on RAB phosphorylation.

Cogo, Susanna / Ho, Franz Y / Tosoni, Elena / Tomkins, James E / Tessari, Isabella / Iannotta, Lucia / Montine, Thomas J / Manzoni, Claudia / Lewis, Patrick A / Bubacco, Luigi / Chartier Harlin, Marie-Christine / Taymans, Jean-Marc / Kortholt, Arjan / Nichols, Jeremy / Cendron, Laura / Civiero, Laura / Greggio, Elisa

Brain research

2022 Volume 1778, Page(s) 147781

Abstract: ... in LRRK2 is the coexistence of GTPase/Roc (Ras of complex) and kinase catalytic functions, bridged by a COR ... supporting a crosstalk between GTPase and kinase domains. In addition, biochemical and structural data ... relevant for the regulation of cytoskeletal dynamics and intracellular trafficking pathways. Among the well ...

Abstract	Leucine-rich repeat kinase 2 (LRRK2) has taken center stage in Parkinson's disease (PD) research as mutations cause familial PD and more common variants increase lifetime risk for disease. One unique feature in LRRK2 is the coexistence of GTPase/Roc (Ras of complex) and kinase catalytic functions, bridged by a COR (C-terminal Of Roc) platform for dimerization. Multiple PD mutations are located within the Roc/GTPase domain and concomitantly lead to defective GTPase activity and augmented kinase activity in cells, supporting a crosstalk between GTPase and kinase domains. In addition, biochemical and structural data highlight the importance of Roc as a molecular switch modulating LRRK2 monomer-to-dimer equilibrium and building the interface for interaction with binding partners. Here we review the effects of PD Roc mutations on LRRK2 function and discuss the importance of Roc as a hub for multiple molecular interactions relevant for the regulation of cytoskeletal dynamics and intracellular trafficking pathways. Among the well-characterized Roc interactors, we focused on the cytoskeletal-related kinase p21-activated kinase 6 (PAK6). We report the affinity between LRRK2-Roc and PAK6 measured by microscale thermophoresis (MST). We further show that PAK6 can modulate LRRK2-mediated phosphorylation of RAB substrates in the presence of LRRK2 wild-type (WT) or the PD G2019S kinase mutant but not when the PD Roc mutation R1441G is expressed. These findings support a mechanism whereby mutations in Roc might affect LRRK2 activity through impaired protein-protein interaction in the cell.
MeSH term(s)	14-3-3 Proteins/metabolism ; GTP Phosphohydrolases/metabolism ; Humans ; Leucine-Rich Repeat Serine-Threonine Protein Kinase-2/metabolism ; Parkinson Disease/metabolism ; Phosphorylation ; Protein Interaction Domains and Motifs ; p21-Activated Kinases/metabolism
Chemical Substances	14-3-3 Proteins ; LRRK2 protein, human (EC 2.7.11.1) ; Leucine-Rich Repeat Serine-Threonine Protein Kinase-2 (EC 2.7.11.1) ; PAK6 protein, human (EC 2.7.11.1) ; p21-Activated Kinases (EC 2.7.11.1) ; GTP Phosphohydrolases (EC 3.6.1.-)
Language	English
Publishing date	2022-01-10
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1200-2
ISSN	1872-6240 ; 0006-8993
ISSN (online)	1872-6240
ISSN	0006-8993
DOI	10.1016/j.brainres.2022.147781
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Zs.A 161: Show issues

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Article ; Online: Primary cilia, A-kinase anchoring proteins and constitutive activity at the orphan G protein-coupled receptor GPR161: A tale about a tail.

Patel, Kinjal / Smith, Nicola J

British journal of pharmacology

2023

Abstract: ... terminus such as PKA phosphorylation sites and an A-kinase anchoring protein motif, which may influence ... which acts as a master regulator of ciliary protein transit and is essential for normal embryonic development ... In this review, we introduce GPR161 in the context of Shh signalling and describe the unique features on its C ...

Abstract	Primary cilia are non-motile antennae-like structures responsible for sensing environmental changes in most mammalian cells. Ciliary signalling is largely mediated by the Sonic Hedgehog (Shh) pathway, which acts as a master regulator of ciliary protein transit and is essential for normal embryonic development. One particularly important player in primary cilia is the orphan G protein-coupled receptor, GPR161. In this review, we introduce GPR161 in the context of Shh signalling and describe the unique features on its C-terminus such as PKA phosphorylation sites and an A-kinase anchoring protein motif, which may influence the function of the receptor, cAMP compartmentalisation and/or trafficking within primary cilia. We discuss the recent putative pairing of GPR161 and spexin-1, highlighting the additional steps needed before GPR161 could be considered 'deorphanised'. Finally, we speculate that the marked constitutive activity and unconventional regulation of GPR161 may indicate that the receptor may not require an endogenous ligand.
Language	English
Publishing date	2023-02-11
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	80081-8
ISSN	1476-5381 ; 0007-1188
ISSN (online)	1476-5381
ISSN	0007-1188
DOI	10.1111/bph.16053
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Article: Control of G protein-coupled receptor function via membrane-interacting intrinsically disordered C-terminal domains.

Mancinelli, Chiara / Marx, Dagan C / Gonzalez-Hernandez, Alberto J / Huynh, Kevin / Mancinelli, Lucia / Arefin, Anisul / Khelashvilli, George / Levitz, Joshua / Eliezer, David

bioRxiv : the preprint server for biology

2024

Abstract: ... coupling to intracellular transducers including heterotrimeric G proteins, GPCR kinases (GRKs), and ... by CTD-membrane interactions in live cells, which may be subject to regulation by CTD phosphorylation and ... related family C GPCRs, metabotropic glutamate receptor 2 (mGluR2) and mGluR3, bind to membranes and ...

Abstract	G protein-coupled receptors (GPCRs) control intracellular signaling cascades via agonist-dependent coupling to intracellular transducers including heterotrimeric G proteins, GPCR kinases (GRKs), and arrestins. In addition to their critical interactions with the transmembrane core of active GPCRs, all three classes of transducers have also been reported to interact with receptor C-terminal domains (CTDs). An underexplored aspect of GPCR CTDs is their possible role as lipid sensors given their proximity to the membrane. CTD-membrane interactions have the potential to control the accessibility of key regulatory CTD residues to downstream effectors and transducers. Here we report that the CTDs of two closely related family C GPCRs, metabotropic glutamate receptor 2 (mGluR2) and mGluR3, bind to membranes and that this interaction can regulate receptor function. We first characterize CTD structure with NMR spectroscopy, revealing lipid composition-dependent modes of membrane binding. Using molecular dynamics simulations and structure-guided mutagenesis, we then identify key conserved residues and cancer-associated mutations that modulate CTD-membrane binding. Finally, we provide evidence that mGluR3 transducer coupling is controlled by CTD-membrane interactions in live cells, which may be subject to regulation by CTD phosphorylation and changes in membrane composition. This work reveals a novel mechanism of GPCR modulation, suggesting that CTD-membrane binding may be a general regulatory mode throughout the broad GPCR superfamily.
Language	English
Publishing date	2024-05-02
Publishing country	United States
Document type	Preprint
DOI	10.1101/2023.08.16.553551
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Article ; Online: Potential Role of Protein Kinase FAM20C on the Brain in Raine Syndrome, an In Silico Analysis.

Palma-Lara, Icela / García Alonso-Themann, Patricia / Pérez-Durán, Javier / Godínez-Aguilar, Ricardo / Bonilla-Delgado, José / Gómez-Archila, Damián / Espinosa-García, Ana María / Nolasco-Quiroga, Manuel / Victoria-Acosta, Georgina / López-Ornelas, Adolfo / Serrano-Bello, Juan Carlos / Olguín-García, María Guadalupe / Palacios-Reyes, Carmen

International journal of molecular sciences

2023 Volume 24, Issue 10

Abstract: FAM20C (family with sequence similarity 20, member C) is a serine/threonine-specific protein kinase ... that is ubiquitously expressed and mainly associated with biomineralization and phosphatemia regulation ... involved signaling pathways and diseases. The BioGRID and Human Protein Atlas databases, the Gorilla tool ...

Abstract	FAM20C (family with sequence similarity 20, member C) is a serine/threonine-specific protein kinase that is ubiquitously expressed and mainly associated with biomineralization and phosphatemia regulation. It is mostly known due to pathogenic variants causing its deficiency, which results in Raine syndrome (RNS), a sclerosing bone dysplasia with hypophosphatemia. The phenotype is recognized by the skeletal features, which are related to hypophosphorylation of different FAM20C bone-target proteins. However, FAM20C has many targets, including brain proteins and the cerebrospinal fluid phosphoproteome. Individuals with RNS can have developmental delay, intellectual disability, seizures, and structural brain defects, but little is known about FAM20C brain-target-protein dysregulation or about a potential pathogenesis associated with neurologic features. In order to identify the potential FAM20C actions on the brain, an in silico analysis was conducted. Structural and functional defects reported in RNS were described; FAM20C targets and interactors were identified, including their brain expression. Gene ontology of molecular processes, function, and components was completed for these targets, as well as for potential involved signaling pathways and diseases. The BioGRID and Human Protein Atlas databases, the Gorilla tool, and the PANTHER and DisGeNET databases were used. Results show that genes with high expression in the brain are involved in cholesterol and lipoprotein processes, plus axo-dendritic transport and the neuron part. These results could highlight some proteins involved in the neurologic pathogenesis of RNS.
MeSH term(s)	Humans ; Protein Kinases/metabolism ; Microcephaly/genetics ; Brain/metabolism ; Protein Serine-Threonine Kinases/metabolism ; Extracellular Matrix Proteins/genetics ; Extracellular Matrix Proteins/metabolism ; Casein Kinase I/genetics ; Casein Kinase I/metabolism
Chemical Substances	Protein Kinases (EC 2.7.-) ; Protein Serine-Threonine Kinases (EC 2.7.11.1) ; Extracellular Matrix Proteins ; FAM20C protein, human (EC 2.7.11.1) ; Casein Kinase I (EC 2.7.11.1)
Language	English
Publishing date	2023-05-17
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms24108904
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