Abstract
Simple SummaryCBL mutations are progressively being described as involved in different clinical manifestations. Somatic CBL mutations can be found in different type of cancer. The clinical spectrum of germline mutations configures the so-called CBL syndrome, a cancer-predisposing condition that includes multisystemic involvement characterized by variable phenotypic expression and expressivity. In this review we provide an up-to-date review of the clinical manifestation of CBL mutations and of the molecular mechanisms in which CBL exerts its pathogenic role.CBL plays a key role in different cell pathways, mainly related to cancer onset and progression, hematopoietic development and T cell receptor regulation. Somatic CBL mutations have been reported in a variety of malignancies, ranging from acute myeloid leukemia to lung cancer. Growing evidence have defined the clinical spectrum of germline CBL mutations configuring the so-called CBL syndrome; a cancer-predisposing condition that also includes multisystemic involvement characterized by variable phenotypic expression and expressivity. This review provides a comprehensive overview of the molecular mechanisms in which CBL exerts its function and describes the clinical manifestation of CBL mutations in humans.
Highlights
IntroductionLarge-scale genomic studies have uncovered a genetic predisposition in a large variety of cancers, especially in children [1]
Over the last years, large-scale genomic studies have uncovered a genetic predisposition in a large variety of cancers, especially in children [1]
Casitas B lineage lymphoma (CBL) has been reported to play a role in different well-known cell pathways, many of those are related to cancer onset and progression, hematopoietic development and T cell receptor regulation
Summary
Large-scale genomic studies have uncovered a genetic predisposition in a large variety of cancers, especially in children [1]. AClBhLalaf nodf tCheBpLr-obtsehinasr,einacdlduidtiinognaaluabreiqausiotifnh-aosmsooclioagtiyonin(UthBeAC)-dteormmaiinnal half of the proteins, including a ubiquitin-association (UBA) domain and more extensive proline and tyrosine-rich regions, which can be phosphorylated and mediate interactions with Src homology region 2 and 3 (SH2 and SH3) domain-containing proteins including GRB2, CD2AP/CIN85, Cool/Pix and p85 subunit of PI3K [12]. These domains play a Cancers 2022, 14, x FOR PEER REVIEW. The E3 ubiquitin ligase activity primarily depends on the RF domain, the intact linker sequence is considered structurally essential for an efficient ubiquitinylation to occur [14]
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