Nicotinate-Nucleotide Pyrophosphorylase (QPRT) belongs to the nadC/modD family. QPRT plays an improtant role in catabolism of quinolinate which acts as a potent endogenous exitotoxin to neurons. In addition, QPRT serves as an an intermediate in the Tryptophan-Nicotinamide Adenine Dinucleotide pathway. QPRT participates in some pathways including Cofactor biosynthesis, NAD(+) biosynthesis and the Nicotinate D-Ribonucleotide from Quinolinate. In addition, QPRT is involved in the catabolism of Quinolinic Acid (QA). The activity toward QA is slightly repressed by phosphoribosylpyrophosphate (PRPP) in both a competitive and a non-competitive manner.
Regulates endocytic recycling. May exert its functions by interacting with multiple effector proteins in different complexes. Acts as a major regulator of membrane delivery during cytokinesis. Together with MYO5B and RAB8A participates in epithelial cell polarization. Together with RAB3IP, RAB8A, the exocyst complex, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis (By similarity). Together with MYO5B participates in CFTR trafficking to the plasma membrane and TF (Transferrin) recycling in nonpolarized cells. Required in a complex with MYO5B and RAB11FIP2 for the transport of NPC1L1 to the plasma membrane. Participates in the sorting and basolateral transport of CDH1 from the Golgi apparatus to the plasma membrane. Regulates the recycling of FCGRT (receptor of Fc region of monomeric Ig G) to basolateral membranes.
The two recurrent dominant mutations in RAB11B leading to a neurodevelopmental syndrome, likely caused by altered GDP/GTP binding that inactivate the protein and induce GEF binding and protein mislocalization.
Plays a role in cytotoxic granule exocytosis in lymphocytes. Required for both granule maturation and granule docking and priming at the immunologic synapse.
Members of the Rab protein family; including RAB27B; are prenylated; membrane-bound proteins involved in vesicular fusion and trafficking (Chen et al.; 1997 [PubMed 9066979]).
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