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CD79B

Official Full Name
CD79b molecule
Organism
Homo sapiens
GeneID
974
Background
The B lymphocyte antigen receptor is a multimeric complex that includes the antigen-specific component, surface immunoglobulin (Ig). Surface Ig non-covalently associates with two other proteins, Ig-alpha and Ig-beta, which are necessary for expression and function of the B-cell antigen receptor. This gene encodes the Ig-beta protein of the B-cell antigen component. Alternatively spliced transcript variants encoding different isoforms have been described. [provided by RefSeq, Jul 2008]
Synonyms
B29; IGB; AGM6; Igbeta;
Bio Chemical Class
Immunoglobulin
Protein Sequence
MARLALSPVPSHWMVALLLLLSAEPVPAARSEDRYRNPKGSACSRIWQSPRFIARKRGFTVKMHCYMNSASGNVSWLWKQEMDENPQQLKLEKGRMEESQNESLATLTIQGIRFEDNGIYFCQQKCNNTSEVYQGCGTELRVMGFSTLAQLKQRNTLKDGIIMIQTLLIILFIIVPIFLLLDKDDSKAGMEEDHTYEGLDIDQTATYEDIVTLRTGEVKWSVGEHPGQE
Open
Disease
Autoimmune disease, Diffuse large B-cell lymphoma, Follicular lymphoma, Malignant haematopoietic neoplasm, Mature B-cell lymphoma
Approved Drug
1 +
Clinical Trial Drug
4 +
Discontinued Drug
0

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Detailed Information

Crucially important for the B-cell receptor (BCR) complex, the CD79b gene codes for a protein component that is crucial in the immune system, especially in B cell signaling and activation. Key participants in the adaptive immune response, B cells depend on the BCR to identify antigens and start intracellular signaling pathways producing immunological reactions.

Structure and Function of CD79b

Comprising a membrane-bound immunoglobulin (Ig) molecule connected with two signaling proteins, CD79b is a component of the BCR complex. Two heavy and two light chains make up the membrane-bound Ig; they are very essential for antigen binding. Non-covalently coupled with the Ig molecule, CD79a and CD79b function as components of signal transduction. Especially, CD79b together with CD79a starts the intracellular signaling cascade following antigen attachment to the Ig component of the BCR. Differentiation, proliferation, and B cell activation all depend on this intricate process.

Src-family kinases phosphorylate the immunoreceptor tyrosine-based activation motif (ITAM) found in the cytoplasmic tails of CD79a and CD79b. Recruiting additional signaling molecules, like SYK (spleen tyrosine kinase), which activates downstream pathways including the PI3K/AKT, NF-κB, and MAPK paths depends on this phosphorylation event. Among the many biological activities that signaling cascades control are B cell survival, activation, differentiation, and metabolism.

Fascinatingly, while their function in BCR assembly and signaling is preserved, the extracellular domains of CD79a and CD79b are very different across species. Cryo-electron microscopy among other recent structural studies has given a thorough understanding of the arrangement of the BCR and its interaction with CD79a/CD79b heterodimers, therefore clarifying the molecular processes behind BCR functioning.

Figure 1 describes the key components and signaling pathways involved in B-cell receptor signaling through CD79a/CD79b in normal B cells.Figure 1. Role of CD79a/CD79b in B-cell receptor signaling in normal B cells. (Tkachenko A, et al., 2023)

Clinical Relevance of CD79b

Particularly those involving B cells, the CD79b gene has been associated with various disorders. Agammaglobulinemia is one such illness, a rare immunodeficiency disease marked by an inability to generate antibodies, therefore compromising the body's defenses against infections. A lack of B cell activation and consequent immune system abnormalities follow from defective BCR signaling arising from mutations in the CD79b gene.

Apart from immunodeficiency, CD79b is also linked to B-cell malignancies like diffuse large B-cell lymphoma (DLBCL). Highly expressed on the surface of B cells in these lymphomas, CD79b is a target of great attraction for treatment approaches. Given medicines that block BCR signaling may cause cell death in B cell lymphoma cells, targeting CD79b in B cell malignancies has shown potential. This has created the road for the creation of fresh treatment approaches meant to alter BCR signaling pathways.

CD79b and BCR Signal Transduction

BCR signaling is critical for the regulation of B cell fate. Upon antigen binding, the BCR undergoes internalization, and its components are trafficked to late endosomes, where antigen processing and presentation occur. Key to the BCR complex's organization and stability as well as its signaling capability is the heterodimer CD79a/CD79b. Important for receptor stability and function, studies have shown that CD79a/CD79b heterodimers control the transport of IgM, stabilize BCR assembly, and enable glycosylation—which helps to stabilize BCR assembly.

Additionally involved in antigenic stimulation and consequent B cell survival is CD79b. Together with signals from other co-receptors including CD40, BAFFR (B-cell activating factor), and TLRs (Toll-like receptors), BCR signaling controls class-switch recombination and antibody synthesis. The adaptive immune response depends on this mechanism as it lets B cells produce antibodies of many isotypes, thereby improving their capacity to combat diverse diseases.

Moreover, CD79b participates in the control of autophagy, a cellular mechanism controlling metabolic balance and survival. Activation of BCR signals mobilization of autophagy-related proteins, which helps to polarise B cells, control trafficking, and enable survival. Maintaining the balance between immunological activation and tolerance depends on this mechanism, which also guarantees that B cells avoid becoming autoreactive or supporting autoimmune disorders.

Phosphorylation, Ubiquitination, and Glycosylation in BCR Signaling

Control of BCR signaling depends critically on post-translational changes of CD79b including glycosylation, ubiquitination, and phosphorylation. Starting downstream signaling from ITAMs on the cytoplasmic tails of CD79a and CD79b requires phosphorylation of those molecules. Src-family kinases, including Lyn and Fyn, phosphorylated SYK and other downstream signaling molecules, therefore activating several pathways controlling B cell activation and survival.

Moreover, important in the control of BCR signaling is the ubiquitination of CD79b. This change may change the localization and trafficking of the BCR complex, therefore affecting its interaction with other signaling molecules and guaranteeing appropriate signal transduction. Crucial for the stability and trafficking of the BCR is the glycosylation of CD79b and IgM, thus guaranteeing that it reaches the cell surface in an active state competent of mediating antigen recognition.

Tightly controlled and with great impact on B cell function are these post-translational changes. Like in the case of mutations in CD79b, dysregulation of these systems might cause immunological malfunction or the growth of B cell cancers.

References:

  1. Tkachenko A, Kupcova K, Havranek O. B-Cell Receptor Signaling and Beyond: The Role of Igα (CD79a)/Igβ (CD79b) in Normal and Malignant B Cells. Int J Mol Sci. 2023;25(1):10.
  2. Xu PP, Shen R, Shi ZY, et al. The Prognostic Significance of CD79B Mutation in Diffuse Large B-Cell Lymphoma: A Meta-analysis and Systematic Literature Review. Clin Lymphoma Myeloma Leuk. 2022;22(12):e1051-e1058.e1.
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