| Primary Identifier | IPR041815 | Type | Family |
| Short Name | Rab35 |
| description | Ras-related protein Rab35 is a member of the large Rab GTPase family. Rab35 is involved in many cellular functions, including endocytic recycling, cytokinesisis and endosomal trafficking []. It is one of several Rab proteins to be found to participate in the regulation of osteoclast cells in rats []. In addition, Rab35 has been identified as a protein that interacts with nucleophosmin-anaplastic lymphoma kinase (NPM-ALK) in human cells. Overexpression of NPM-ALK is a key oncogenic event in some anaplastic large-cell lymphomas; since Rab35 interacts with NPM-ALK, it may provide a target for cancer treatments []. Rabs are regulated by GTPase activating proteins (GAPs), which interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins [, ]. |
