CADM1 promotes malignant features of small-cell lung cancer by recruiting 4.1R to the plasma membrane

Funaki, Toko; Ito, Takeshi; Tanei, Zen‐ichi; Goto, Akiteru; Niki, Toshiro; Matsubara, Daisuke; Murakami, Yoshinori

doi:10.1016/j.bbrc.2020.11.121

Cited by 10 publications

(13 citation statements)

References 28 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The 4.1 protein binding motif of CADM1 in the cytoplasmic domain promotes colony formation. Furthermore, knockdown of 4.1R inhibits CADM1 mediated colony formation (Funaki et al, 2021). In addition, clinical data suggest that membrane colocalization of CADM1 and 4.1R is associated with higher tumor stage, and CADM1-4.1R complex contributes to SCLC malignancy.…”

Section: Respiratory Systemmentioning

confidence: 94%

See 1 more Smart Citation

Functional and Clinical Characteristics of Cell Adhesion Molecule CADM1 in Cancer

Gao

Zhang

2021

Front. Cell Dev. Biol.

View full text Add to dashboard Cite

The cell adhesion molecule CADM1, which participates in cell adhesion and signal transduction, has a regulatory effect on the development of tumors. CADM1 is often involved in malignant tumors of multiple organ systems, such as the respiratory and digestive systems. Upregulated CADM1 promotes tumor cell apoptosis and inhibits malignant proliferation. Along with cell cycle-related proteins, it participates in regulating signaling pathways, such as EMT, STAT3, and AKT, and plays an important role in inhibiting invasion and migration. Considering clinical characteristics, low CADM1 expression is associated with aggressive tumors and poor prognosis. In addition, some long non-coding RNAs (lncRNAs) or miRNAs directly or indirectly act on CADM1 to regulate tumor growth and motility. Interestingly, CADM1 function differs in adult T-cell leukemia/lymphoma (ATLL), and NF-κB is thought to be involved in this process. Taken together, CADM1 could be a potential biomarker for early diagnosis and a target for cancer treatment in future clinical practices.

show abstract

Section: Respiratory Systemmentioning

confidence: 94%

“…Small cell lung cancer is an aggressive, high-grade, neuroendocrine tumor. It has been identified that 80% of SCLC cells retain higher CADM1 expression (Funaki et al, 2021). The 4.1 protein binding motif of CADM1 in the cytoplasmic domain promotes colony formation.…”

Section: Respiratory Systemmentioning

confidence: 99%

Functional and Clinical Characteristics of Cell Adhesion Molecule CADM1 in Cancer

Gao

Zhang

2021

Front. Cell Dev. Biol.

View full text Add to dashboard Cite

show abstract

“…The 4.1N–CAM3 interaction is likely to link the F-action cytoskeleton, leading to the regulation of the synaptic architecture and the function in the nervous system ( Zhou et al, 2005 ). 4.1R–CAM1 interaction is recently verified in small-cell lung cancer (SCLC) ( Funaki et al, 2021 ). In SCLC cells NCI-H446, 4.1N, 4.1R, and 4.1G are expressed at the cell–cell contact sites and colocalized with CAM1.…”

Section: 1n In the Nerve Systemmentioning

confidence: 95%

“…Loss of 4.1B in the axon is associated with reduced levels of CAM1 and CAM3 ( Einheber et al, 2013 ). 4.1B and 4.1N are identified as specific CAM1 effector molecules for the recruitment of N-methyl-D-aspartate receptors and AMPARs to adhesion sites of synapses during synapse formation, respectively ( Funaki et al, 2021 ). Protein 4.1 family members exhibit substantial homologies in the FERM (72–81% identity), SAB (53–66% identity), and CT (72–74% identity) domains ( Parra et al, 2004 ).…”

Section: 1n In the Nerve Systemmentioning

confidence: 99%

“…In SCLC cells NCI-H446, 4.1N, 4.1R, and 4.1G are expressed at the cell–cell contact sites and colocalized with CAM1. In CAM1-knockout NCI-H446 cells, 4.1R expression at the intercellular junctions is lost but localization of 4.1N and 4.1G is not affected, suggesting that 4.1R, but not 4.1N or 4.1G, is recruited to the cell membrane in a CAM1-dependent manner ( Funaki et al, 2021 ).…”

Section: 1n In the Nerve Systemmentioning

confidence: 99%

See 1 more Smart Citation

4.1N-Mediated Interactions and Functions in Nerve System and Cancer

Yang

Liu

Wang

2021

Front. Mol. Biosci.

View full text Add to dashboard Cite

Scaffolding protein 4.1N is a neuron-enriched 4.1 homologue. 4.1N contains three conserved domains, including the N-terminal 4.1-ezrin-radixin-moesin (FERM) domain, internal spectrin–actin–binding (SAB) domain, and C-terminal domain (CTD). Interspersed between the three domains are nonconserved domains, including U1, U2, and U3. The role of 4.1N was first reported in the nerve system. Then, extensive studies reported the role of 4.1N in cancers and other diseases. 4.1N performs numerous vital functions in signaling transduction by interacting, locating, supporting, and coordinating different partners and is involved in the molecular pathogenesis of various diseases. In this review, recent studies on the interactions between 4.1N and its contactors (including the α7AChr, IP3R1, GluR1/4, GluK1/2/3, mGluR8, KCC2, D2/3Rs, CASK, NuMA, PIKE, IP6K2, CAM 1/3, βII spectrin, flotillin-1, pp1, and 14-3-3) and the 4.1N-related biological functions in the nerve system and cancers are specifically and comprehensively discussed. This review provides critical detailed mechanistic insights into the role of 4.1N in disease relationships.

show abstract

Efficient intracellular drug delivery by co-administration of two antibodies against cell adhesion molecule 1

Hagiyama,

Yoneshige,

Wada

et al. 2024

Journal of Controlled Release

View full text Add to dashboard Cite

CADM1 promotes malignant features of small-cell lung cancer by recruiting 4.1R to the plasma membrane

Cited by 10 publications

References 28 publications

Functional and Clinical Characteristics of Cell Adhesion Molecule CADM1 in Cancer

Functional and Clinical Characteristics of Cell Adhesion Molecule CADM1 in Cancer

4.1N-Mediated Interactions and Functions in Nerve System and Cancer

Efficient intracellular drug delivery by co-administration of two antibodies against cell adhesion molecule 1

Contact Info

Product

Resources

About