RAB14 is a member of the RAS oncogene family, which is known for its role in intracellular membrane trafficking. This protein is part of the large RAB family of low molecular mass GTPases, which act as molecular switches that flip between an inactive GDP-bound state and an active GTP-bound state. This switching mechanism is crucial for recruiting downstream effector proteins onto membranes, thereby facilitating various cellular processes .
The RAB14 gene is a protein-coding gene that plays a significant role in several cellular pathways, including the innate immune system and vesicle-mediated transport. Gene Ontology (GO) annotations related to this gene include GTP binding and GDP binding. An important paralog of this gene is RAB4A .
The small GTPases Rab, including RAB14, are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. RAB14 cycles between an inactive GDP-bound form and an active GTP-bound form, which is able to recruit different sets of downstream effectors directly responsible for vesicle formation, movement, tethering, and fusion .
RAB14 is involved in membrane trafficking between the Golgi complex and endosomes during early embryonic development. It regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. RAB14 may act by modulating the kinesin KIF16B-cargo association to endosomes .
Additionally, RAB14 regulates, together with its guanine nucleotide exchange factor DENND6A, the specific endocytic transport of ADAM10, N-cadherin/CDH2 shedding, and cell-cell adhesion. It mediates endosomal tethering and fusion through the interaction with RUFY1 and RAB4B .
RAB14 has been identified as an oncogene and is associated with the proliferation of gastric cancer cells. It is the last member of the Rab11 subfamily and has been identified together with Rab5, Rab7, and Rab1 in the proteome of endosomes isolated from migrating cells. There have been few reports on the association between RAB14 and human cancers, but its role as an oncogene highlights its potential importance in cancer research .