Abstract: Eukaryotic cells divide their metabolic labor between functionally distinct, membrane-enveloped organelles, each precisely tailored for a specific set of biochemical reactions. Peroxisomes are ubiquitous, endoplasmic reticulum-derived organelles that perform requisite biochemical functions intimately connected to lipid metabolism. Upon cell division, cells have to strictly control peroxisome division and inheritance to maintain an appropriate number of peroxisomes in each cell. Peroxisome division follows a specific sequence of events that include: peroxisome elongation, membrane constriction and peroxisome fission. Pex11 proteins mediate the elongation step of peroxisome division, while the final fission is executed by dynamin-related proteins. The mechanisms responsible for peroxisome membrane constriction are poorly understood. Molecular players involved in peroxisome inheritance are just beginning to be elucidated. Inp1p and Inp2p are two recently identified peroxisomal proteins that perform antagonistic functions in regulating peroxisome inheritance in budding yeast. Inp1p promotes the retention of peroxisomes in mother cells and buds by attaching them to as of yet unidentified cortical structures. Inp2p is implicated in the motility of peroxisomes by linking peroxisomes to the Myo2p motor, which then propels their movement along actin cables. The functions of Inp1p and Inp2p are cell cycle-regulated and coordinated to ensure a fair distribution of peroxisomes at cytokinesis. Expected final online publication date for the Annual Review of Cell and Developmental Biology Volume 23 is October 6, 2007. Please see http://www.annualreviews.org/catalog/pubdates.aspx for revised estimates.