Chapter Five - Ubiquitination of Ion Channels and Transporters

Lamothe, Shawn M.; Zhang, Shetuan

doi:10.1016/bs.pmbts.2016.02.005

Cited by 23 publications

(19 citation statements)

References 377 publications

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“…Although both dTAG molecules and d9A series of PROTACs are based on hijacking the CRL4 CRBN ligase, we assume that other E3 ligases can also be recruited to SLCs. In fact, we can foresee the development of degraders that harness E3 ligases that are thought to be involved in membrane protein proteostasis, such as NEDD4/NEDD4L (Goel et al, 2015;Lamothe and Zhang, 2016;MacGurn et al, 2012). To exploit targeted protein degradation, a binding event that per se may not lead to any change in protein function can be the basis for a degrader and even utilized to engineer selectivity.…”

Section: Discussionmentioning

confidence: 99%

Targeted Degradation of SLC Transporters Reveals Amenability of Multi-Pass Transmembrane Proteins to Ligand-Induced Proteolysis

Bensimon

Pizzagalli

Kartnig

et al. 2020

Cell Chemical Biology

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Section: Discussionmentioning

confidence: 99%

Targeted Degradation of SLC Transporters Reveals Amenability of Multi-Pass Transmembrane Proteins to Ligand-Induced Proteolysis

Bensimon

Pizzagalli

Kartnig

et al. 2020

Cell Chemical Biology

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“…However, the expression of Kcnj4 and Kcnh2 was regulated from low level at day 7 to high level at day 15, but Kcnj3 was highly expressed around mesodermal stage. We also noted the expression difference between transcription and translation levels for GIRK1, KIR3.4, KCNE1, and KIR2.1 during the differentiation, which may attribute to the dynamic status of the channels that are constantly renewed by ubiquitination at early stage of heart development [Lamothe and Zhang, ]. These results indicate that the combination expression of potassium channels are really involved lineage commitment and cardiomyocyte differentiation, even though the details need to be further clarified.…”

Section: Disscussionmentioning

confidence: 77%

Regulation of Histone Acetylation on Expression Profiles of Potassium Channels During Cardiomyocyte Differentiation From Mouse Embryonic Stem Cells

Wang

Liu

et al. 2017

J of Cellular Biochemistry

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The cardiomyocyte differentiation from mouse embryonic stem cells (mESCs) is a dynamic and complex process that involved in the precision regulation of histone acetylation. The formation of action potential (AP) in mature cardiomyocytes is based on the expression pattern of Na , Ca , and K ion channels, in which the slow delayed rectifier potassium current (I ), the rapid delayed rectifier potassium current (I ) and the inwardly rectifying Kir current (I ) mainly contribute to repolarization for AP in different species. However, the expression status of potassium channels conducted I , I , and I in cardiomyocyte differentiation are not fully defined. Here, we investigated the expression pattern of the slow delayed rectifier potassium channel and the rapid delayed rectifier potassium channel using a model of mouse cardiomyocyte differentiation under different conditions of histone acetylation. We found that expression levels of both the delayed rectifier potassium channel and the inwardly rectifying potassium channel were more sensitive to histone hyperacetylation during differentiation from mESCs into cardiomyocytes. Especially, histone H4 hyperacetylation induced by Class I HDACs inhibitors promoted the expression profiles of potassium channels (Kcnj2, Kcnj3, Kcnj5, Kcnj11, and Kcnh2) in the process. Our results provide a clue for expression status of potassium channels which may be essential to forming functional cardiomyocyte in the cardiac lineage commitment of mESC. J. Cell. Biochem. 118: 4460-4467, 2017. © 2017 Wiley Periodicals, Inc.

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“…When Ca 2+ binds to the C2 domain, the HECT domain is exposed and Nedd4-2 is activated. Activated Nedd4-2 binds to the PY motifs of target proteins through its WW domains for ubiquitination (Lamothe and Zhang, 2016). Ion channels tagged with ubiquitin are usually compartmentalized into vesicles destined for degradation (by the lysosomal or proteasomal system) or recycled back to the membrane via small GTPase Rabs.…”

Section: Proteasome Degradation Pathwaymentioning

confidence: 99%

Life Cycle of the Cardiac Voltage-Gated Sodium Channel NaV1.5

Dong

et al. 2020

Front. Physiol.

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Cardiac voltage-gated sodium channel NaV1.5, encoded by SCN5A, is crucial for the upstroke of action potential and excitation of cardiomyocytes. NaV1.5 undergoes complex processes before it reaches the target membrane microdomains and performs normal functions. A variety of protein partners are needed to achieve the balance between SCN5A transcription and mRNA decay, endoplasmic reticulum retention and export, Golgi apparatus retention and export, selective anchoring and degradation, activation, and inactivation of sodium currents. Subtle alterations can impair NaV1.5 in terms of expression or function, eventually leading to NaV1.5-associated diseases such as lethal arrhythmias and cardiomyopathy.

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Chapter Five - Ubiquitination of Ion Channels and Transporters

Cited by 23 publications

References 377 publications

Targeted Degradation of SLC Transporters Reveals Amenability of Multi-Pass Transmembrane Proteins to Ligand-Induced Proteolysis

Targeted Degradation of SLC Transporters Reveals Amenability of Multi-Pass Transmembrane Proteins to Ligand-Induced Proteolysis

Regulation of Histone Acetylation on Expression Profiles of Potassium Channels During Cardiomyocyte Differentiation From Mouse Embryonic Stem Cells

Life Cycle of the Cardiac Voltage-Gated Sodium Channel NaV1.5

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