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Article: Nephronophthisis-associated FBW7 mediates cyst-dependent decline of renal function in ADPKD.

Patel, Maulin Mukeshchandra / Gerakopoulos, Vasileios / Petsouki, Eleni / Zimmerman, Kurt A / Tsiokas, Leonidas

bioRxiv : the preprint server for biology

2024

Abstract: Nephronophthisis (NPHP) and autosomal dominant Polycystic Kidney Disease (ADPKD) are two genetically distinct forms of Polycystic Kidney Disease (PKD), yet both diseases present with kidney cysts and a gradual decline in renal function. Prevailing dogma ... ...

Abstract	Nephronophthisis (NPHP) and autosomal dominant Polycystic Kidney Disease (ADPKD) are two genetically distinct forms of Polycystic Kidney Disease (PKD), yet both diseases present with kidney cysts and a gradual decline in renal function. Prevailing dogma in PKD is that changes in kidney architecture account for the decline in kidney function, but the molecular/cellular basis of such coupling is unknown. To address this question, we induced a form of proteome reprogramming by deleting
Language	English
Publishing date	2024-03-02
Publishing country	United States
Document type	Preprint
DOI	10.1101/2024.02.29.582788
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Article ; Online: Insights into the Regulation of Ciliary Disassembly.

Patel, Maulin M / Tsiokas, Leonidas

Cells

2021 Volume 10, Issue 11

Abstract: The primary cilium, an antenna-like structure that protrudes out from the cell surface, is present in most cell types. It is a microtubule-based organelle that serves as a mega-signaling center and is important for sensing biochemical and mechanical ... ...

Abstract	The primary cilium, an antenna-like structure that protrudes out from the cell surface, is present in most cell types. It is a microtubule-based organelle that serves as a mega-signaling center and is important for sensing biochemical and mechanical signals to carry out various cellular processes such as proliferation, migration, differentiation, and many others. At any given time, cilia length is determined by a dynamic balance of cilia assembly and disassembly processes. Abnormally short or long cilia can cause a plethora of human diseases commonly referred to as ciliopathies, including, but not limited to, skeletal malformations, obesity, autosomal dominant polycystic kidney disease, retinal degeneration, and bardet-biedl syndrome. While the process of cilia assembly is studied extensively, the process of cilia disassembly and its biological role(s) are less well understood. This review discusses current knowledge on ciliary disassembly and how different cellular processes and molecular signals converge to carry out this process. This information will help us understand how the process of ciliary disassembly is regulated, identify the key steps that need further investigation, and possibly design therapeutic targets for a subset of ciliopathies that are causally linked to defective ciliary disassembly.
MeSH term(s)	Animals ; Cilia/metabolism ; Humans ; Microtubules/metabolism ; Models, Biological ; Polymerization ; Signal Transduction
Language	English
Publishing date	2021-11-01
Publishing country	Switzerland
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	2661518-6
ISSN	2073-4409 ; 2073-4409
ISSN (online)	2073-4409
ISSN	2073-4409
DOI	10.3390/cells10112977
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Article ; Online: Insights into the Regulation of Ciliary Disassembly

Maulin M. Patel / Leonidas Tsiokas

Cells, Vol 10, Iss 2977, p

2021 Volume 2977

Abstract	The primary cilium, an antenna-like structure that protrudes out from the cell surface, is present in most cell types. It is a microtubule-based organelle that serves as a mega-signaling center and is important for sensing biochemical and mechanical signals to carry out various cellular processes such as proliferation, migration, differentiation, and many others. At any given time, cilia length is determined by a dynamic balance of cilia assembly and disassembly processes. Abnormally short or long cilia can cause a plethora of human diseases commonly referred to as ciliopathies, including, but not limited to, skeletal malformations, obesity, autosomal dominant polycystic kidney disease, retinal degeneration, and bardet-biedl syndrome. While the process of cilia assembly is studied extensively, the process of cilia disassembly and its biological role(s) are less well understood. This review discusses current knowledge on ciliary disassembly and how different cellular processes and molecular signals converge to carry out this process. This information will help us understand how the process of ciliary disassembly is regulated, identify the key steps that need further investigation, and possibly design therapeutic targets for a subset of ciliopathies that are causally linked to defective ciliary disassembly.
Keywords	cilia ; cilia disassembly ; ciliopathies ; Biology (General) ; QH301-705.5
Subject code	650
Language	English
Publishing date	2021-11-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Polycystins as components of large multiprotein complexes of polycystin interactors.

Hardy, Emily / Tsiokas, Leonidas

Cellular signalling

2020 Volume 72, Page(s) 109640

Abstract: Naturally occurring mutations in two separate genes, PKD1 and PKD2, are responsible for the vast majority of all cases of autosomal dominant polycystic kidney disease (ADPKD), one of the most common genetic diseases affecting 1 in 1000 Americans. The ... ...

Abstract	Naturally occurring mutations in two separate genes, PKD1 and PKD2, are responsible for the vast majority of all cases of autosomal dominant polycystic kidney disease (ADPKD), one of the most common genetic diseases affecting 1 in 1000 Americans. The hallmark of ADPKD is the development of epithelial cysts in the kidney, liver, and pancreas. PKD1 encodes a large plasma membrane protein (PKD1, PC1, or Polycystin-1) with a long extracellular domain and has been speculated to function as an atypical G protein coupled receptor. PKD2 encodes an ion channel of the Transient Receptor Potential superfamily (TRPP2, PKD2, PC2, or Polycystin-2). Despite the identification of these genes more than 20 years ago, the molecular function of their encoded proteins and the mechanism(s) by which mutations in PKD1 and PKD2 cause ADPKD remain elusive. Genetic, biochemical, and functional evidence suggests they form a multiprotein complex present in multiple locations in the cell, including the plasma membrane, endoplasmic reticulum, and the primary cilium. Over the years, numerous interacting proteins have been identified using directed and unbiased approaches, and shown to modulate function, cellular localization, and protein stability and turnover of Polycystins. Delineation of the molecular composition of the Polycystin complex can have a significant impact on understanding their cellular function in health and disease states and on the identification of more specific and effective therapeutic targets.
MeSH term(s)	Actin Cytoskeleton/metabolism ; Animals ; GTP-Binding Proteins/metabolism ; Humans ; Multiprotein Complexes/chemistry ; Multiprotein Complexes/metabolism ; Protein Binding ; Signal Transduction ; TRPP Cation Channels/chemistry ; TRPP Cation Channels/metabolism
Chemical Substances	Multiprotein Complexes ; TRPP Cation Channels ; GTP-Binding Proteins (EC 3.6.1.-)
Language	English
Publishing date	2020-04-17
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1002702-6
ISSN	1873-3913 ; 0898-6568
ISSN (online)	1873-3913
ISSN	0898-6568
DOI	10.1016/j.cellsig.2020.109640
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Article ; Online: The inhibitor of MyoD Family A (I-MFA) regulates megakaryocyte lineage commitment and terminal differentiation.

Houser, Jeremy S / Patel, Maulin / Wright, Kyle / Onopiuk, Marta / Tsiokas, Leonidas / Humphrey, Mary Beth

Blood cells, molecules & diseases

2023 Volume 102, Page(s) 102760

Abstract: Hematopoiesis and lineage commitment are regulated by several conserved cell-intrinsic signaling pathways, including MAPKs and β-catenin/TCF/LEF. The Inhibitor of MyoD Family A (I-MFA), a transcriptional repressor and tumor suppressor gene, interacts ... ...

Abstract	Hematopoiesis and lineage commitment are regulated by several conserved cell-intrinsic signaling pathways, including MAPKs and β-catenin/TCF/LEF. The Inhibitor of MyoD Family A (I-MFA), a transcriptional repressor and tumor suppressor gene, interacts with these pathways and is dysregulated in chronic and acute myeloid leukemias, suggesting it may play a role in development and differentiation during hematopoiesis. To study this, immune cell populations in the bone marrow (BM) and periphery were analyzed in mice lacking Mdfi, encoding I-MFA (I-MFA-/-), and wild type (WT) controls. I-MFA-/- mice had reduced spleen and BM cellularity, with significant hyposplenism, compared to WT mice. In blood, total red blood cells and platelet counts were significantly reduced in I-MFA-/- mice, accompanied by a reduction in megakaryocyte (MK)/erythrocyte progenitor cells and an increase in myeloid progenitors in BM compared to WT mice. The K562 cell line exhibits PMA-induced MK differentiation, and shRNA knockdown of I-MFA resulted in reduced differentiation compared to control, with an increase and prolongation in phospho-JNK and phospho-ERK signaling. Overexpression of I-MFA promoted MK differentiation. These results suggest I-MFA plays a cell-intrinsic role in the response to differentiation signals, an effect that can be explored in the context of hematological cancers or other blood proliferative disorders.
MeSH term(s)	Mice ; Animals ; Megakaryocytes ; Bone Marrow/metabolism ; Cell Differentiation ; Hematopoiesis ; Bone Marrow Cells/pathology ; Cell Lineage
Language	English
Publishing date	2023-05-27
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1237083-6
ISSN	1096-0961 ; 1079-9796
ISSN (online)	1096-0961
ISSN	1079-9796
DOI	10.1016/j.bcmd.2023.102760
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Article ; Online: Correction to "Gold Nanoparticles Inhibit Macropinocytosis by Decreasing KRAS Activation".

Elechalawar, Chandra Kumar / Rao, Geeta / Gulla, Suresh Kumar / Patel, Maulin Mukeshchandra / Frickenstein, Alex / Means, Nicolas / Roy, Ram Vinod / Tsiokas, Leonidas / Asfa, Sima / Panja, Prasanta / Rao, Chinthalapally / Wilhelm, Stefan / Bhattacharya, Resham / Mukherjee, Priyabrata

ACS nano

2024 Volume 18, Issue 12, Page(s) 9242

Language	English
Publishing date	2024-03-11
Publishing country	United States
Document type	Published Erratum
ISSN	1936-086X
ISSN (online)	1936-086X
DOI	10.1021/acsnano.4c01293
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Article ; Online: Loss of polycystins suppresses deciliation via the activation of the centrosomal integrity pathway.

Gerakopoulos, Vasileios / Ngo, Peter / Tsiokas, Leonidas

Life science alliance

2020 Volume 3, Issue 9

Abstract: The primary cilium is a microtubule-based, antenna-like organelle housing several signaling pathways. It follows a cyclic pattern of assembly and deciliation (disassembly and/or shedding), as cells exit and re-enter the cell cycle, respectively. In ... ...

Abstract	The primary cilium is a microtubule-based, antenna-like organelle housing several signaling pathways. It follows a cyclic pattern of assembly and deciliation (disassembly and/or shedding), as cells exit and re-enter the cell cycle, respectively. In general, primary cilia loss leads to kidney cystogenesis. However, in animal models of autosomal dominant polycystic kidney disease, a major disease caused by mutations in the
MeSH term(s)	Animals ; Centrosome/metabolism ; Cilia/metabolism ; Cilia/physiology ; Disease Models, Animal ; Female ; Kidney/pathology ; Male ; Mice ; Mice, Inbred C57BL ; Mitosis/physiology ; Mutation ; NIH 3T3 Cells ; Polycystic Kidney Diseases/genetics ; Polycystic Kidney, Autosomal Dominant/genetics ; Signal Transduction ; TRPP Cation Channels/genetics ; TRPP Cation Channels/metabolism ; Tumor Suppressor Protein p53 ; Tumor Suppressor p53-Binding Protein 1 ; Ubiquitin Thiolesterase
Chemical Substances	TRPP Cation Channels ; Tumor Suppressor Protein p53 ; Tumor Suppressor p53-Binding Protein 1 ; USP28 protein, mouse ; polycystic kidney disease 1 protein ; polycystic kidney disease 2 protein ; Ubiquitin Thiolesterase (EC 3.4.19.12)
Language	English
Publishing date	2020-07-10
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ISSN	2575-1077
ISSN (online)	2575-1077
DOI	10.26508/lsa.202000750
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Article ; Online: Function and regulation of TRPP2 at the plasma membrane.

Tsiokas, Leonidas

American journal of physiology. Renal physiology

2009 Volume 297, Issue 1, Page(s) F1–9

Abstract: The vast majority (approximately 99%) of all known cases of autosomal dominant polycystic kidney disease (ADPKD) are caused by naturally occurring mutations in two separate, but genetically interacting, loci, pkd1 and pkd2. pkd1 encodes a large ... ...

Abstract	The vast majority (approximately 99%) of all known cases of autosomal dominant polycystic kidney disease (ADPKD) are caused by naturally occurring mutations in two separate, but genetically interacting, loci, pkd1 and pkd2. pkd1 encodes a large multispanning membrane protein (PKD1) of unknown function, while pkd2 encodes a protein (TRPP2, polycystin-2, or PKD2) of the transient receptor potential (TRP) superfamily of ion channels. Biochemical, functional, and genetic studies support a model in which PKD1 physically interacts with TRPP2 to form an ion channel complex that conveys extracellular stimuli to ionic currents. However, the molecular identity of these extracellular stimuli remains elusive. Functional studies in cell culture show that TRPP2 can be activated in response to mechanical cues (fluid shear stress) and/or receptor tyrosine kinase (RTK) and G protein-coupled receptor (GPCR) activation at the cell surface. Recent genetic studies in Chlamydomonas reinhardtii show that CrPKD2 functions in a pathway linking cell-cell adhesion and Ca(2+) signaling. The mode of activation depends on protein-protein interactions with other channel subunits and auxiliary proteins. Therefore, understanding the mechanisms underlying the molecular makeup of TRPP2-containing complexes is critical in delineating the mechanisms of TRPP2 activation and, most importantly, the mechanisms by which naturally occurring mutations in pkd1 or pkd2 lead not only to ADPKD, but also to other defects reported in model organisms lacking functional TRPP2. This review focuses on the molecular assembly, function, and regulation of TRPP2 as a cell surface cation channel and discusses its potential role in Ca(2+) signaling and ADPKD pathophysiology.
MeSH term(s)	Animals ; Calcium Signaling/physiology ; Cell Membrane/physiology ; Humans ; Mutation/genetics ; Polycystic Kidney, Autosomal Dominant/genetics ; Polycystic Kidney, Autosomal Dominant/physiopathology ; TRPP Cation Channels/genetics ; TRPP Cation Channels/physiology
Chemical Substances	TRPP Cation Channels ; polycystic kidney disease 2 protein
Language	English
Publishing date	2009-02-25
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	603837-2
ISSN	1522-1466 ; 0363-6127
ISSN (online)	1522-1466
ISSN	0363-6127
DOI	10.1152/ajprenal.90277.2008
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Article ; Online: FBW7 couples structural integrity with functional output of primary cilia.

Petsouki, Eleni / Gerakopoulos, Vasileios / Szeto, Nicholas / Chang, Wenhan / Humphrey, Mary Beth / Tsiokas, Leonidas

Communications biology

2021 Volume 4, Issue 1, Page(s) 1066

Abstract: Structural defects in primary cilia have robust effects in diverse tissues and systems. However, how disorders of ciliary length lead to functional outcomes are unknown. We examined the functional role of a ciliary length control mechanism of FBW7- ... ...

Abstract	Structural defects in primary cilia have robust effects in diverse tissues and systems. However, how disorders of ciliary length lead to functional outcomes are unknown. We examined the functional role of a ciliary length control mechanism of FBW7-mediated destruction of NDE1, in mesenchymal stem cell (MSC) differentiation. We show that FBW7 functions as a master regulator of both negative (NDE1) and positive (TALPID3) regulators of ciliogenesis, with an overall positive net effect on primary cilia formation, MSC differentiation to osteoblasts, and bone architecture. Deletion of Fbxw7 suppresses ciliation, Hedgehog activity, and differentiation, which are partially rescued in Fbxw7/Nde1-null cells. We also show that NDE1, despite suppressing ciliogenesis, promotes MSC differentiation by increasing the activity of the Hedgehog pathway by direct binding and enhancing GLI2 activity in a cilia-independent manner. We propose that FBW7 controls a protein-protein interaction network coupling ciliary structure and function, which is essential for stem cell differentiation.
MeSH term(s)	Animals ; Cell Differentiation ; Cilia/metabolism ; F-Box-WD Repeat-Containing Protein 7/genetics ; F-Box-WD Repeat-Containing Protein 7/metabolism ; Male ; Mice ; Microtubule-Associated Proteins/genetics ; Microtubule-Associated Proteins/metabolism ; Signal Transduction
Chemical Substances	F-Box-WD Repeat-Containing Protein 7 ; Fbxw7 protein, mouse ; Microtubule-Associated Proteins ; Nde1 protein, mouse
Language	English
Publishing date	2021-09-13
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ISSN	2399-3642
ISSN (online)	2399-3642
DOI	10.1038/s42003-021-02504-4
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Article ; Online: Gold Nanoparticles Inhibit Macropinocytosis by Decreasing KRAS Activation.

ACS nano

2023 Volume 17, Issue 10, Page(s) 9326–9337

Abstract: The RAS-transformed cells utilize macropinocytosis to acquire amino acids to support their uncontrolled growth. However, targeting RAS to inhibit macropinocytosis remains a challenge. Here, we report that gold nanoparticles (GNP) inhibit macropinocytosis ...

Abstract	The RAS-transformed cells utilize macropinocytosis to acquire amino acids to support their uncontrolled growth. However, targeting RAS to inhibit macropinocytosis remains a challenge. Here, we report that gold nanoparticles (GNP) inhibit macropinocytosis by decreasing KRAS activation. Using surface-modified and unmodified GNP, we showed that unmodified GNP specifically sequestered both wild-type and mutant KRAS and inhibited its activation, irrespective of growth factor stimulation, while surface-passivated GNP had no effect. Alteration of KRAS activation is reflected on downstream signaling cascades, macropinocytosis and tumor cell growth
MeSH term(s)	Humans ; Gold/pharmacology ; Proto-Oncogene Proteins p21(ras)/genetics ; Metal Nanoparticles ; Pinocytosis ; Pancreatic Neoplasms/pathology ; Cell Proliferation ; Cell Line, Tumor ; Mutation
Chemical Substances	Gold (7440-57-5) ; Proto-Oncogene Proteins p21(ras) (EC 3.6.5.2) ; KRAS protein, human
Language	English
Publishing date	2023-05-02
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, N.I.H., Extramural
ISSN	1936-086X
ISSN (online)	1936-086X
DOI	10.1021/acsnano.3c00920
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