CEMIP
CEMIP (cell migration inducing hyaluronidase 1) is a hyaluronan-binding protein that depolymerises hyaluronic acid through the clathrin-coated pit endocytic pathway. It is also known as KIAA1199, HYBID, TMEM2L and CEMIP1. Browse Assay Genie's current range of CEMIP research reagents below, or read on for the biology behind the target.
CEMIP binds hyaluronic acid (HA) and mediates its depolymerisation via the cell membrane-associated clathrin-coated pit endocytic pathway. It hydrolyses high molecular weight hyaluronic acid to produce an intermediate-sized product, a process that may occur through rapid vesicle endocytosis and recycling, without intracytoplasmic accumulation or digestion in lysosomes. The protein is involved in hyaluronan catabolism in the dermis of the skin and in arthritic synovium, and it may also be involved in hearing.
Beyond matrix turnover, CEMIP positively regulates epithelial-mesenchymal transition (EMT), and through this tumour cell growth, invasion and cancer dissemination. In collaboration with HSPA5/BIP, it promotes cancer cell migration in a calcium- and PKC-dependent manner. Gene Ontology annotation also lists clathrin heavy chain binding, hyalurononglucosaminidase activity, positive regulation of protein phosphorylation and positive regulation of protein targeting to membrane.
UniProt records CEMIP in the nucleus, cytoplasm, endoplasmic reticulum, cell membrane, clathrin-coated pits and the secreted compartment. The CEMIP gene belongs to the HGNC hyaluronidases group and the protein belongs to the CEMIP family. The gene was formerly named KIAA1199, and earlier descriptive names were cell migration inducing protein, hyaluronan binding. The mouse ortholog is Cemip. Researchers studying the CEMIP protein or CEMIP gene often use it as a model for non-lysosomal hyaluronan breakdown.
CEMIP depolymerises high molecular weight hyaluronic acid via clathrin-coated pits, making it a focus for studies of extracellular matrix turnover.
CEMIP positively regulates EMT and promotes tumour cell growth, invasion and dissemination, and works with HSPA5/BIP to drive migration.
The protein contributes to hyaluronan catabolism in the dermis and in arthritic synovium, relevant to tissue remodelling research.
CEMIP binds clathrin heavy chain and acts through rapid vesicle endocytosis and recycling, offering a route into membrane trafficking studies.
CEMIP binds hyaluronic acid and mediates its depolymerisation through the clathrin-coated pit endocytic pathway, producing intermediate-sized fragments from high molecular weight hyaluronan. It also positively regulates epithelial-mesenchymal transition and, with HSPA5/BIP, promotes calcium- and PKC-dependent cancer cell migration.
CEMIP stands for cell migration inducing hyaluronidase 1. Aliases and previous symbols include KIAA1199, HYBID, CEMIP1, TMEM2L and IR2155535. Its earlier names were cell migration inducing protein, hyaluronan binding, and cell migration inducing hyaluronan binding protein. UniProt lists it as Cell migration-inducing and hyaluronan-binding protein.
A mouse ortholog, Cemip, is recorded, so rodent models are available for study. UniProt links CEMIP to hyaluronan catabolism in skin and arthritic synovium, to cancer cell invasion and dissemination through EMT, and possibly to hearing. Check the datasheet of any product for its validated reactivity.
Other hyaluronidases, hyaluronan pathway proteins and migration-associated targets with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q8WUJ3; product specifications from Assay Genie datasheets.