ArticleAmerican journal of physiology. Cell physiology2013
Carboxy terminus and pore-forming domain properties specific to Cx37 are necessary for Cx37-mediated suppression of insulinoma cell proliferation.
Article in American journal of physiology. Cell physiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 29 citations in OpenAlex.
- Connexin 37 sequestering of activated-ERK in the cytoplasm promotes p27-mediated endothelial cell cycle arrest.Life science alliance · 2023Article
- An Analysis Regarding the Association Between Connexins and Colorectal Cancer (CRC) Tumor Microenvironment.Journal of inflammation research · 2022Article
- Expression of Connexin43 Stimulates Endothelial Angiogenesis Independently of Gap Junctional Communication In Vitro.International journal of molecular sciences · 2021Article
- Cutaneous and hepatic vascular lesions due to a recurrent somaticHGG advances · 2021Article
- Connexins in Cancer: Jekyll or Hyde?Biomolecules · 2020Review
- Serine 319 phosphorylation is necessary and sufficient to induce a Cx37 conformation that leads to arrested cell cycling.Journal of cell science · 2020Article
- Phosphorylation-Dependent Intra-Domain Interaction of the Cx37 Carboxyl-Terminus Controls Cell Survival.Cancers · 2019Article
- Cx43 Channel Gating and Permeation: Multiple Phosphorylation-Dependent Roles of the Carboxyl Terminus.International journal of molecular sciences · 2018Article
- Connexin43 Carboxyl-Terminal Domain Directly Interacts with β-Catenin.International journal of molecular sciences · 2018Article
- Protein⁻Protein Interactions with Connexin 43: Regulation and Function.International journal of molecular sciences · 2018Review
- Shear-induced Notch-Cx37-p27 axis arrests endothelial cell cycle to enable arterial specification.Nature communications · 2017Article
- Regulation of Cx37 channel and growth-suppressive properties by phosphorylation.Journal of cell science · 2017Article
- Chemical shift assignments of the connexin37 carboxyl terminal domain.Biomolecular NMR assignments · 2017Article
- Connexin and pannexin channels in cancer.BMC cell biology · 2016Review
- Secondary structural analysis of the carboxyl-terminal domain from different connexin isoforms.Biopolymers · 2016Article
- Determinants of Cx43 Channel Gating and Permeation: The Amino Terminus.Biophysical journal · 2016Article
- Degradation of gap junction connexins is regulated by the interaction with Cx43-interacting protein of 75 kDa (CIP75).The Biochemical journal · 2015Article
- Structural determinants and proliferative consequences of connexin 37 hemichannel function in insulinoma cells.The Journal of biological chemistry · 2014Article
- High bone mass in mice lacking Cx37 because of defective osteoclast differentiation.The Journal of biological chemistry · 2014Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Connexin 37 (Cx37) suppresses cell proliferation when expressed in rat insulinoma (Rin) cells, an effect also manifest in vivo during vascular development and in response to tissue injury. Mutant forms of Cx37 with nonfunctional channels but normally localized, wild-type carboxy termini are not growth suppressive. Here we determined whether the carboxy-terminal (CT) domain is required for Cx37-mediated growth suppression and whether the Cx37 pore-forming domain can be replaced with the Cx43 pore-forming domain and still retain growth-suppressive properties. We show that despite forming functional gap junction channels and hemichannels, Cx37 with residues subsequent to 273 replaced with a V5-epitope tag (Cx37-273tr*V5) had no effect on the proliferation of Rin cells, did not facilitate G1-cell cycle arrest with serum deprivation, and did not prolong cell cycle time comparably to the wild-type protein. The chimera Cx43*CT37, comprising the pore-forming domain of Cx43 and CT of Cx37, also did not suppress proliferation, despite forming functional gap junctions with a permselective profile similar to wild-type Cx37. Differences in channel behavior of both Cx37-273tr*V5 and Cx43*CT37 relative to their wild-type counterparts and failure of the Cx37-CT to interact as the Cx43-CT does with the Cx43 cytoplasmic loop suggest that the Cx37-CT and pore-forming domains are both essential to growth suppression by Cx37.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.