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Originally published as MBC in Press, 10.1091/mbc.E03-06-0413 on December 10, 2003

Vol. 15, Issue 2, 815-826, February 2004

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A Unique Region of RILP Distinguishes It from Its Related Proteins in Its Regulation of Lysosomal Morphology and Interaction with Rab7 and Rab34

Tuanlao Wang, Ka Khuen Wong, and Wanjin Hong *

Membrane Biology Laboratory, Institute of Molecular and Cell Biology, Singapore 117609, Singapore

Submitted June 18, 2003; Revised October 6, 2003; Accepted October 6, 2003
Monitoring Editor: Keith Mostov

Rab7 and Rab34 are implicated in regulation of lysosomal morphology and they share a common effector referred to as the RILP (Rab-interacting lysosomal protein). Two novel proteins related to RILP were identified and are tentatively referred to as RLP1 and RLP2 (for RILP-like protein 1 and 2, respectively). Overexpression of RILP caused enlarged lysosomes that are positioned more centrally in the cell. However, the morphology and distribution of lysosomes were not affected by overexpression of either RLP1 or RLP2. The molecular basis for the effect of RILP on lysosomes was investigated, leading to the demonstration that a 62-residue region (amino acids 272-333) of RILP is necessary for RILP's role in regulating lysosomal morphology. Remarkably, transferring this 62-residue region unique to RILP into corresponding sites in RLP1 rendered the chimeric protein capable of regulating lysosome morphology. A correlation between the interaction with GTP-bound form of both Rab proteins and the capability of regulating lysosomes was established. These results define a unique region in RILP responsible for its specific role in regulating lysosomal morphology as well as in its interaction with Rab7 and Rab34.

Article published online ahead of print. Mol. Biol. Cell 10.1091/mbc.E03-06-0413. Article and publication date are available at www.molbiolcell.org/cgi/doi/10.1091/mbc.E03-06-0413.

* Corresponding author. E-mail address: mcbhwj{at}imcb.a-star.edu.sg.




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