Liprin-beta-1 (IPR030437)

Short name: PPFIBP1

Overlapping homologous superfamilies


Family relationships


Liprin-beta-1 is a member of the LAR (leukocyte common antigen-related) protein tyrosine phosphatase-interacting protein (liprin) family [PMID: 9624153]. Liprin-beta-1 interacts with metastasis-associated protein S100A4 (Mts1), and this interaction results in the inhibition of liprin-beta-1 phosphorylation by protein kinase C and protein kinase CK2 in vitro [PMID: 11836260]. In Xenopus, it plays a role in the maintenance of lymphatic vessel integrity [PMID: 19965622].

Liprin was originally identified as binding partners of the receptor protein tyrosine phosphatase LAR (leukocyte common antigen-related), which functions in axon guidance and mammary gland development [PMID: 9624153]. In vertebrates, there are two families of liprins, liprin-alpha and liprin-beta, which have four (alpha1-4) and two (beta1-2) members. Liprins contain an N-terminal coiled-coil domain and a C-terminal liprin homology (LH) region comprised of three sterile alpha motif (SAM) domains. The N-terminal coiled coils of liprin-alpha act as binding regions for several synaptic protein, while the SAM repeats can bind to both phosphatases and protein kinases [PMID: 21855798]. The autophosphorylation of liprin regulates its association with LAR [PMID: 16313174]. Interestingly, all Liprin-alpha genes are subject to alternative splicing, which is regulated in a developmental manner [PMID: 19013515]. The structure of the human CASK/liprin-alpha/liprin-beta ternary complex has been revealed [PMID: 21855798].

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.