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These cells are derived from the same granulocyte\/monocyte progenitors and share multiple receptors except those that are cell\u2010specific. In both types of cells, all known receptors reside in lipid rafts, form multiprotein complexes with recruited signaling molecules, and are internalized upon receptor engagement. Signal transduction proceeds in a chain of protein phosphorylations, where adaptor protein LAT (linker\u2010for\u2010activation\u2010of\u2010T\u2010cells) plays a central role. The key kinase that associates LAT phosphorylation and lipid raft internalization is Syk (spleen\u2010tyrosine\u2010kinase) and\/or an Src\u2010family\u2010kinase, most probably Lck (lymphocyte\u2010specific\u2010protein\u2010tyrosine\u2010kinase). Dephosphorylation of phosphorylated Syk and Lck by activated SHP\u20101 (Src\u2010homology\u2010region\u20102\u2010domain\u2010containing\u2010phosphatase\u20101) terminates the signal transduction and endocytosis of receptors, resulting in inhibition of osteoclast differentiation and other functions. In malignant plasma cells (MM cells) too, SHP\u20101 plays a similar indispensable role in controlling signal transduction required for survival and proliferation, though BLNK (B\u2010cell\u2010linker\u2010protein), a functional equivalent of LAT and SLP\u201076 (SH2\u2010domain\u2010containing\u2010leukocyte\u2010protein\u2010of\u201076\u2010kDa) in B cells, is used instead of LAT. In both osteoclasts and MM cells, therefore, activated SHP\u20101 acts negatively in receptor\u2010mediated cellular functions. In osteoblasts, however, activated SHP\u20101 promotes differentiation, osteocalcin generation, and mineralization by preventing both downregulation of transcription factors, such as Ostrix and Runx2, and degradation of \u03b2\u2010catenin required for activation of the transcription factors. SHP\u20101 is activated by tyrosine phosphorylation\u00a0and micromolar doses (M\u2010dose) of CCRI\u2010ligand\u2010induced SHP\u20101 activation. Small molecular compounds, such as A770041, Sorafenib, Nitedanib, and Dovitinib, relieve the autoinhibitory conformation. Activation of SHP\u20101 by M\u2010dose CCRI ligands or the compounds described may prevent the progression of bone lesions in MM.<\/jats:p>","DOI":"10.1002\/jcb.29949","type":"journal-article","created":{"date-parts":[[2021,5,10]],"date-time":"2021-05-10T11:46:02Z","timestamp":1620647162000},"page":"1313-1325","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["A possible way to prevent the progression of bone lesions in multiple myeloma via Src\u2010homology\u2010region\u20102\u2010domain\u2010containing\u2010phosphatase\u20101 activation"],"prefix":"10.1002","volume":"122","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-7867-0109","authenticated-orcid":false,"given":"Shiro","family":"Kanegasaki","sequence":"first","affiliation":[{"name":"Department of Lipid Signaling, Research Institute National Center for Global Health and Medicine Tokyo 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