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Determined the solution structure of human synaptotagmin-like protein 4 (Slp4). Through modification of cysteine residues, found Slp4 (show S1PR4 Proteins) binding of two zinc atoms is required for correct folding.
Granuphilin makes granules immobile and fusion-reluctant beneath the plasma membrane. Those granuphilin-positive, docked granules release a portion of granuphilin upon fusion, and fuse at a frequency and time course similar to those of granuphilin-negative undocked granules. Granuphilin forms a 180-nm cluster at the site of each docked granule, along with granuphilin-interacting Rab27a (show RAB27A Proteins) and Munc18-1 (show STXBP1 Proteins) clusters.
GLUT5 required an interaction cascade of Rab11 (show RAB11A Proteins), Myo5B, Slp4a, Munc18-2 (show STXBP2 Proteins), and Vamp7 (show VAMP7 Proteins) with Stx3 (show STX3 Proteins).
Phosphatidylinositol 4,5-bisphosphate binds to the concave surface of granuphilin-C2A domain. The key residues involved in the binding were validated by mutation analysis.
the mechanisms of granuphilin plasma membrane targeting and release
Recruitment of STXBP1 (show STXBP1 Proteins) by the Rab27A (show RAB27A Proteins) effector SYTL4 promotes Weibel-Palade body exocytosis.
Slp4 (show S1PR4 Proteins) and Rab8 (show RAB8A Proteins) are expressed and interact in human platelets, and might be involved in dense granule release.
in insulin (show INS Proteins)-producing cells adequate levels of mir (show MLXIP Proteins)-9 are mandatory for maintaining appropriate Granuphilin levels and optimal secretory capacity
Synaptotagmin-like protein 4 (Slp4)/granuphilin-a contains an N-terminal Slp (show SEPT9 Proteins) homology domain (SHD (show SHD Proteins)) (PMID: 11327731). The SHD (show SHD Proteins) of Slp4 (show S1PR4 Proteins) specifically and directly binds the GTP (show AK3 Proteins)-bound form of Rab3A (show RAB3A Proteins), Rab8 (show RAB8A Proteins), and Rab27A (show RAB27A Proteins).
Granuphilin and exophilin7, differentially regulate the exocytosis of either stably or minimally docked granules, respectively.
granuphilin binds to syntaxin-2 (show STX2 Proteins) and syntaxin-3 (show STX3 Proteins) as well as syntaxin-1a (show STX1A Proteins), it likely mediates granule docking through interactions with those multiple syntaxins on the plasma membrane.
granuphilin promotes the plasma membrane targeting of insulin (show INS Proteins) granules via interaction with syntaxin 1a (show STX1A Proteins)
It is shown that the granuphilin promoter is a target of SREBP-1c (show SREBF1 Proteins), a transcription factor that controls fatty acid synthesis, and MafA (show MAFA Proteins), a beta (show SUCLA2 Proteins) cell differentiation factor
Synaptotagmin-like protein 4 (Slp4)/granuphilin-a contains an N-terminal Slp (show SEPT9 Proteins) homology domain (SHD (show SHD Proteins)) (PMID: 11327731). The SHD (show SHD Proteins) of Slp4 specifically and directly binds the GTP (show AK3 Proteins)-bound form of Rab3A (show RAB3A Proteins), Rab8 (show RAB8A Proteins), and Rab27A (show RAB27A Proteins).
This gene encodes a member of the synaptotagmin like protein family. Members of this family are characterized by an N-terminal Rab27 binding domain and C-terminal tandem C2 domains. The encoded protein binds specific small Rab GTPases and is involved in intracellular membrane trafficking. This protein binds Rab27 and may be involved in inhibiting dense core vesicle exocytosis. Alternate splicing results in multiple transcript variants that encode the same protein.
synaptotagmin-like 4 (granuphilin-a)
, synaptotagmin-like 4
, synaptotagmin-like protein 4
, granuphilin b