ArticleThe Biochemical journal2001
Ca(2+)/calmodulin-dependent protein kinase mediates the phosphorylation of CD44 required for cell migration on hyaluronan.
Article in The Biochemical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
10 citing papers in PubMed, 25 citations in OpenAlex.
- Multifaceted roles of CD44 in cancer progression and targeted therapeutic strategies.Experimental & molecular medicine · 2026Review
- CD44 Intracellular Domain: A Long Tale of a Short Tail.Cancers · 2023Review
- Molecular basis of PIP2-dependent conformational switching of phosphorylated CD44 in binding FERM.Biophysical journal · 2023Article
- Neutrophils promote T-cell activation through the regulated release of CD44-bound Galectin-9 from the cell surface during HIV infection.PLoS biology · 2021Article
- The Role of Calmodulin in Tumor Cell Migration, Invasiveness, and Metastasis.International journal of molecular sciences · 2020Review
- Interleukin-1β-induced Reduction of CD44 Ser-325 Phosphorylation in Human Epidermal Keratinocytes Promotes CD44 Homomeric Complexes, Binding to Ezrin, and Extended, Monocyte-adhesive Hyaluronan Coats.The Journal of biological chemistry · 2015Article
- The liberation of CD44 intracellular domain modulates adenoviral vector transgene expression.The Journal of biological chemistry · 2012Article
- Directional sensing of a phorbol ester gradient requires CD44 and is regulated by CD44 phosphorylation.Oncogene · 2006Article
- Cellular and molecular parameters of mesothelioma.Journal of cellular biochemistry · 2006Review
- CD44 modulates Smad1 activation in the BMP-7 signaling pathway.The Journal of cell biology · 2004Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
CD44 is the principal cell surface receptor for the extracellular matrix glycosaminoglycan hyaluronan, and binding to this ligand underlies CD44-mediated cell attachment and migration. As would be expected for a widely expressed adhesion receptor, CD44 is subject to complex regulatory events, and mis-regulation of the receptor has been associated with a number of disease pathologies, including chronic inflammatory conditions and the progression of metastatic tumours. In previous studies we have demonstrated that a key control point for this receptor is the phosphorylation of CD44 on a conserved cytoplasmic serine residue, Ser(325). This modification is not required for efficient ligand binding, but is an essential component of CD44-dependent cell migration on a hyaluronan substratum. To understand better the mechanism regulating CD44 phosphorylation on Ser(325), we have generated a monoclonal antibody that specifically recognizes CD44 phosphorylated on Ser(325), and have developed assays to identify the Ser(325) kinase. We demonstrate here that CD44 is phosphorylated to high stoichiometry in resting cells and that Ca(2+)/calmodulin-dependent protein kinase II is a CD44 Ser(325) kinase.
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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.