ArticleThe Biochemical journal2005
ADP-ribosylation of integrin alpha7 modulates the binding of integrin alpha7beta1 to laminin.
Article in The Biochemical journal, 2005. 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, 39 citations in OpenAlex.
- The ADP-ribosyltransferases 3 (ART3) is a novel suppressor of pathological cardiac hypertrophy by ribosylating ITGA7.Acta pharmaceutica Sinica. B · 2026Article
- From Bench to Clinic: The 2024 FASEB Scientific Research Conference on NAD Metabolism and Signaling.Molecular medicine (Cambridge, Mass.) · 2025Article
- Nicotinamide riboside kinases regulate skeletal muscle fiber-type specification and are rate-limiting for metabolic adaptations during regeneration.Frontiers in cell and developmental biology · 2022Article
- NMRK2 Gene Is Upregulated in Dilated Cardiomyopathy and Required for Cardiac Function and NAD Levels during Aging.International journal of molecular sciences · 2021Article
- p75NTR optimizes the osteogenic potential of human periodontal ligament stem cells by up-regulating α1 integrin expression.Journal of cellular and molecular medicine · 2020Article
- A need for NAD+ in muscle development, homeostasis, and aging.Skeletal muscle · 2018Review
- Effect of ART1 on the proliferation and migration of mouse colon carcinoma CT26 cells in vivo.Molecular medicine reports · 2017Article
- Tubb3 regulation by the Erk and Akt signaling pathways: a mechanism involved in the effect of arginine ADP-ribosyltransferase 1 (Art1) on apoptosis of colon carcinoma CT26 cells.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2016Article
- ART1 promotes starvation-induced autophagy: a possible protective role in the development of colon carcinoma.American journal of cancer research · 2015Article
- Nicotinamide phosphoribosyltransferase can affect metastatic activity and cell adhesive functions by regulating integrins in breast cancer.DNA repair · 2014Article
- ADP-ribosylation of arginine.Amino acids · 2011Review
- Integrin activation promotes axon growth on inhibitory chondroitin sulfate proteoglycans by enhancing integrin signaling.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2011Article
- Nrk2b-mediated NAD+ production regulates cell adhesion and is required for muscle morphogenesis in vivo: Nrk2b and NAD+ in muscle morphogenesis.Developmental biology · 2010Article
- Acheron, a Lupus antigen family member, regulates integrin expression, adhesion, and motility in differentiating myoblasts.American journal of physiology. Cell physiology · 2010Article
- Basal and inducible expression of the thiol-sensitive ART2.1 ecto-ADP-ribosyltransferase in myeloid and lymphoid leukocytes.Purinergic signalling · 2009Article
- Genetically determined proteolytic cleavage modulates alpha7beta1 integrin function.The Journal of biological chemistry · 2008Article
- Identification of two regulatory binding sites which confer myotube specific expression of the mono-ADP-ribosyltransferase ART1 gene.BMC molecular biology · 2008Article
- Extracellular NAD and ATP: Partners in immune cell modulation.Purinergic signalling · 2007Article
- Purification and molecular cloning of a DNA ADP-ribosylating protein, CARP-1, from the edible clam Meretrix lamarckii.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The extracellular domain of integrin alpha7 is ADP-ribosylated by an arginine-specific ecto-ADP-ribosyltransferase after adding exogenous NAD+ to intact C2C12 skeletal muscle cells. The effect of ADP-ribosylation on the structure or function of integrin alpha7beta1 has not been explored. In the present study, we show that ADP-ribosylation of integrin alpha7 takes place exclusively in differentiated myotubes and that this post-translational modification modulates the affinity of alpha7beta1 dimer for its ligand, laminin. ADP-ribosylation in the 37-kDa 'stalk' region of alpha7 that takes place at micromolar NAD+ concentrations increases the binding of the alpha7beta1 dimer to laminin. Increased in vitro binding of integrin alpha7beta1 to laminin after ADP-ribosylation of the 37-kDa fragment of alpha7 requires the presence of Mn2+ and it is not observed in the presence of Mg2+. In contrast, ADP-ribosylation of the 63-kDa N-terminal region comprising the ligand-binding site of alpha7 that occurs at approx. 100 microM NAD+ inhibits the binding of integrin alpha7beta1 to laminin. Furthermore, incubation of C2C12 myotubes with NAD+ increases the expression of an epitope on integrin beta1 subunit recognized by monoclonal antibody 9EG7. We discuss our results based on the current models of integrin activation. We also hypothesize that ADP-ribosylation may represent a mechanism of regulation of integrin alpha7beta1 function in myofibres in vivo when the continuity of the membrane is compromised and NAD+ is available as a substrate for ecto-ADP-ribosylation.
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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.