The composition of reticular adhesions in RPMI-7951 and MDA-MB-435S melanoma cell lines and its comparison with the reticular adhesion composition following talin2 or KANK2 knockdown

ABSTRACT: Integrins bind extracellular matrix proteins and, when clustered, form integrin adhesion complexes (IACs) that connect to and regulate the cytoskeleton, shaping normal and tumour cell behaviour. In addition to well-known nascent adhesions, focal adhesions (FAs), fibrillar adhesions (FBs), and hemidesmosomes, a newer class of IACs, reticular adhesions (RAs), has been identified. RAs, originally described as flat clathrin lattices formed by integrin αVβ5, are unique in lacking actin association and FA markers. Their roles in normal and cancer cells remain unclear. We previously showed that two melanoma cell lines, MDA-MB-435S and RPMI-7951, rely primarily on integrin αVβ5 for adhesion. Here, we provide a detailed analysis of RAs in these lines, which differ in their ability to form FBs. To define RA composition, we disrupted FAs using the actin polymerization inhibitor cytochalasin D, isolated RAs, and analysed them by MS-based proteomics. Known RA-associated proteins, including the AP-2 adaptor complex, disabled homolog 2 (DAB2) and Numb were identified in both lines, along with talin2. Notably, we also detected the presence of KN motif and ankyrin repeat domains protein (KANK2) in RA isolates. We then investigated the effect of talin2 or KANK2 knockdown on RAs composition.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Melanocyte, Cell Culture

DISEASE(S): Skin Melanoma

SUBMITTER: Nikolina Stojanovic  

LAB HEAD: Andreja Ambriović-Ristov

PROVIDER: PXD071922 | Pride | 2026-06-15

REPOSITORIES: Pride